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(2E)-2-(1H-benzimidazol-2-yl)-3-(3-iodo-4-methoxyphenyl)prop-2-enenitrile
-
-
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
(2E)-3-(2-amino-4-chlorophenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(2-bromo-4-chlorophenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(4-chloro-2-fluorophenyl)-N-hydroxyprop-2-enamide
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-
(2E)-3-(4-chloro-2-hydroxyphenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(4-chloro-2-methoxyphenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(4-chloro-2-methylphenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(4-chloro-2-nitrophenyl)-N-hydroxyprop-2-enamide
-
-
(2E)-3-(4-chlorophenyl)-N-hydroxyprop-2-enamide
-
a trans-cinnamic hydroxamate
(2E)-3-[4-chloro-2-(iminomethyl)phenyl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[4-chloro-2-(methylsulfanyl)phenyl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[4-chloro-2-(methylsulfonyl)phenyl]-N-hydroxyprop-2-enamide
-
-
(2E)-3-[4-chloro-2-(trifluoromethyl)phenyl]-N-hydroxyprop-2-enamide
-
-
(2E)-4-[(7-nitro-9H-fluoren-2-yl)amino]-4-oxobut-2-enoic acid
-
19.5% inhibition at 0.02 mM
(3alpha,5beta,7alpha,12alpha,17alpha)-24-([2-[(7-chloroquinolin-4-yl)amino]ethyl]amino)cholane-3,7,12-triyl triacetate
P10845
90% inhibition at 0.02 mM
(3R)-3-(2,4-dichlorophenyl)-N,5-dihydroxypentanamide
-
-
(3R)-3-(4-chlorophenyl)-N,5-dihydroxypentanamide
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-
(3S)-3-(2,4-dichlorophenyl)-N,5-dihydroxypentanamide
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-
(3S)-3-(4-chlorophenyl)-N,5-dihydroxypentanamide
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-
([[5-[[1-(4-ammoniobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-(3-hydroxyphenyl)thiophen-3-yl]acetyl]amino)oxidanide
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synthesis and binding structure, overview, multiple molecular dynamics simulations of the endopeptidase in complex with inhibitor 2 using the dummy atom approach, overview
1-(2,4-dichlorobenzyl)-1H-pyrrole-2,5-dione
-
inhibitor is providing relatively potent BoNT protection in a cellular assay. It inhibits the biological activity of BoNT/A1 in neuronal cells. This inhibitor is about 7 to 10times more potent than 2-(2,4-dichlorobenzylidene)cyclopent-4-ene-1,3-dione
2'-((9H-fluoren-2-ylamino)carbonyl)-4,4'-bis(hydroxy(oxido)amino)[1,1'-biphenyl]-2-carboxylic acid
-
82% inhibition at 0.02 mM
2'-[(7-fluoro-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
47.6% inhibition at 0.02 mM
2'-[(7-methoxy-9H-fluoren-2-yl)carbamoyl]biphenyl-2-carboxylic acid
-
20.9% inhibition at 0.02 mM
2'-[(9-hydroxy-9H-fluoren-2-yl)carbamoyl]biphenyl-2-carboxylic acid
-
20% inhibition at 0.02 mM
2'-[(9-oxo-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
20.2% inhibition at 0.02 mM
2'-[(9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
37.2% inhibition at 0.02 mM
2(9H-fluorene-2-carbonyl)benzoic acid
-
80.1% inhibition at 0.02 mM
2,2'-(1,4-dioxobutane-1,4-diyl)dibenzoic acid
-
21.2% inhibition at 0.02 mM
2,4-dichlorocinnamic acid hydroxamate
-
-
2,4-dichlorocinnamic hydroxamate
-
binding site and complex structure, overview
2,5-dichlorocyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
2,5-dimethoxy-3-(4-methylphenyl)naphthalene-1,4-dione
A5HZZ9
-
2-(1,2-dihydroacenaphthylene-5-carbonyl)benzoic acid
-
11.5% inhibition at 0.02 mM
2-(1H-benzo[d]imidazol-2-yl)-3-(5-(furan-2-yl)thiophen-2-yl)acrylonitrile
-
-
2-(1H-benzo[d]imidazol-2-yl)-3-(biphenyl-4-yl)acrylonitrile
-
-
2-(2,3-dihydro-1H-indene-5-carbonyl)benzoic acid
-
16.3% inhibition at 0.02 mM
2-(2,4-dichlorobenzylidene)cyclopent-4-ene-1,3-dione
-
inhibits the biological activity of BoNT/A1 in neuronal cells. This inhibitor is about 7 to 10times less potent than 1-(2,4-dichlorobenzyl)-1H-pyrrole-2,5-dione
2-(2,4-dihydroxybenzoyl)benzoic acid
-
14.7% inhibition at 0.02 mM
2-(2-oxo-2,3-dihydro-1,3-benzoxazole-5-carbonyl)benzoic acid
-
35% inhibition at 0.02 mM
2-(3,5-dichloro-2-hydroxybenzoyl)benzoic acid
-
19.2% inhibition at 0.02 mM
2-(3,6-dioxocyclohexa-1,4-dien-1-yl)acetic acid
A5HZZ9
-
2-(3-methyl-5,6,7,8-tetrahydronaphthalene-2-carbonyl)benzoic acid
-
24.8% inhibition at 0.02 mM
2-(4-(2,4-dichlorophenoxy)phenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)-1H-indole
-
-
2-(4-(2-chloro-4-cyanophenoxy)phenyl)-1H-indole-6-carbonitrile
-
-
2-(4-(2-chloro-4-cyanophenoxy)phenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)indole
-
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2-(4-(4-(6-(1,4,5,6-tetrahydropyrimidin-2-yl)benzo[b]thiophen-2-yl)phenoxy)phenyl)-1,4,5,6-tetrahydropyrimidine
-
-
2-(4-(4-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)phenoxy)phenyl)-4,5-dihydro-1H-imidazole
-
-
2-(4-(4-(6-(5-hydroxy-1,4,5,6-tetrahydropyrimidin-2-yl)-1H-indol-2-yl)phenoxy)phenyl)-1,4,5,6-tetrahydropyrimidin-5-ol
-
-
2-(4-(4-carbamoylphenoxy)phenyl)-1H-indole-6-carboxamide
-
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2-(4-(4-cyanophenoxy)phenyl)-1H-indole-6-carboximidamide
-
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2-(4-(4-cyanophenoxy)phenyl)indole-6-carbonitrile
-
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2-(4-(6-(1,4,5,6-tetrahydropyrimidin-2-yl)benzo[b]thiophen-2-yl)phenyl)-1,4,5,6-tetrahydropyrimidine
-
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2-(4-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)-phenyl)-4,5-dihydro-1H-imidazole
-
-
2-(4-carboxybenzoyl)benzoic acid
-
13.7% inhibition at 0.02 mM
2-(4-fluorophenyl)-1H-indole-6-carbonitrile
-
-
2-(4-fluorophenyl)-1H-indole-6-carboxamide
-
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2-(4-fluorophenyl)-1H-indole-6-carboximidamide
-
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2-(4-iodophenyl)cyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
2-(4-methoxyphenyl)-1H-indole-6-carboxamide
-
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2-(4-methoxyphenyl)-1H-indole-6-carboximidamide
-
-
2-(4-methoxyphenyl)-6-(4,5-dihydro-1H-imidazol-2-yl)-1H-indole
-
-
2-(4-methylphenyl)naphthalene-1,4-dione
A5HZZ9
-
2-(5-(4-cyanophenoxy)pyridin-2-yl)-1H-indole-6-carbonitrile
-
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2-(5-fluoro-2-pyridyl)-6-benzo[b]thiophenecarboxamide
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2-(5-{[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl}-2-phenylthiophen-3-yl)-N-hydroxyacetamide
-
i.e. 2-(5-[[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-phenylthiophen-3-yl)-N-hydroxyacetamide
2-(9H-fluorene-2-carbonyl)benzoic acid
-
-
2-(pyridin-2-ylamino)cyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-([1,1'-biphenyl]-4-carbonyl)benzoic acid
-
37.8% inhibition at 0.02 mM
2-amino-N-(4-phenoxyphenyl)acetamide
A5HZZ9
-
2-amino-N-[3-(benzyloxy)phenyl]acetamide
A5HZZ9
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2-benzoylbenzoic acid
-
15.9% inhibition at 0.02 mM
2-bromo-4-chlorocinnamic acid hydroxamate
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2-chlorocyclohexa-2,5-diene-1,4-dione
A5HZZ9
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2-mercapto-3-phenylpropionyl-R
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2-mercapto-3-phenylpropionyl-RA
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2-mercapto-3-phenylpropionyl-RAAKML
-
-
2-mercapto-3-phenylpropionyl-RAT
-
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2-mercapto-3-phenylpropionyl-RATAML
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2-mercapto-3-phenylpropionyl-RATK
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2-mercapto-3-phenylpropionyl-RATKAL
-
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2-mercapto-3-phenylpropionyl-RATKM
-
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2-mercapto-3-phenylpropionyl-RATKML
-
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2-mercapto-3-phenylpropionyl-RATKMLGSG
-
-
2-mercapto-3-phenylpropionyl-RVTKML
-
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2-methoxy-3-(4-methylphenyl)cyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
2-methoxycyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
2-methyl-4-chlorocinnamic acid hydroxamate
-
-
2-methyl-7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
2-methyl-7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
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2-methyl-7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
2-methylcyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
2-methylnaphthalene-1,4-dione
A5HZZ9
-
2-phenylcyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
2-trifluoromethyl-4-chlorocinnamic acid hydroxamate
-
-
2-[(3-bromo-9-oxo-9H-fluoren-2-yl)carbamoyl]cyclohexane-1-carboxylic acid
-
19.3% inhibition at 0.02 mM
2-[(4-bromo-9-oxo-9H-fluoren-2-yl)carbamoyl]benzoic acid
-
26.2% inhibition at 0.02 mM
2-[(9-oxo-9H-fluoren-2-yl)carbamoyl]benzoic acid
-
14.8% inhibition at 0.02 mM
2-[(9-oxo-9H-fluoren-2-yl)carbamoyl]cyclohexane-1-carboxylic acid
-
18.3% inhibition at 0.02 mM
2-[(9H-fluoren-2-yl)carbamoyl]cyclohexane-1-carboxylic acid
-
12% inhibition at 0.02 mM
-
2-[1-cyano-2-(3-bromo-5-methoxy-4-hydroxyphenyl)vinyl]benzimidazole
-
-
2-[1-cyano-2-(3-chloro-5-methoxy-4-hydroxyphenyl)vinyl]benzimidazole
-
-
2-[4-(methylamino)-3-nitrobenzoyl]benzoic acid
-
14.1% inhibition at 0.02 mM
2-[5-{[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl}-2-(3-hydroxyphenyl)thiophen-3-yl]-N-hydroxyacetamide
-
i.e. 2-[5-[[1-(4-aminobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-(3-hydroxyphenyl)thiophen-3-yl]-N-hydroxyacetamide, 79% inhibition of BoNTA at 0.02 mM
2-[5-{[1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indol-6-yl]carbonyl}-2-(3-aminophenyl)thiophen-3-yl]-N-hydroxyacetamide
-
i.e. 2-(5-(1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indole-6-carbonyl)-2-(3-aminophenyl)thiophen-3-yl)-N-hydroxyacetamide, 47% inhibition of BoNTA at 0.02 mM. The hydroxamate coordinates the zinc ion embedded in the active site and forms a hydrogen bond to Glu224. The cation shows pi-interaction of the thiophene-substituted phenyl group with Arg363. Occurence of pi-pi interactions of the thiophene-substituted phenyl group with Phe194 and Tyr366, of interaction of the ketone oxygen atom with Asp370 that is bridged by at least one water molecule, and of cation-pi and pi-pi interactions of the indole-substituted phenyl group with Lys66 and Gln162, respectively
2-[5-{[1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indol-6-yl]carbonyl}-2-(4-hydroxyphenyl)thiophen-3-yl]-N-hydroxyacetamide
-
i.e. 2-(5-(1-(4-aminobutyl)-3-fluoro-2-phenyl-1H-indole-6-carbonyl)-2-(4-hydroxyphenyl)thiophen-3-yl)-N-hydroxyacetamide, 82% inhibition of BoNTA at 0.02 mM. The hydroxamate coordinates the zinc ion embedded in the active site and forms a hydrogen bond to Glu224. The cation shows pi-interaction of the thiophene-substituted phenyl group with Arg363. Occurence of pi-pi interactions of the thiophene-substituted phenyl group with Phe194 and Tyr366, of interaction of the ketone oxygen atom with Asp370 that is bridged by at least one water molecule, and of cation-pi and pi-pi interactions of the indole-substituted phenyl group with Lys66 and Gln162, respectively
2-[[17-oxoestra-1,3,5(10)-trien-3-yl]oxy]cyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
24-mer C-terminal peptide of LcE1
-
the activity of the light chain of botulinum toxin A is significantly reduced to 32% by the peptide with sequence TGRGLVKKIIRFCKNIVSVKGIRK
-
3'-O-ethyl-dynasore
A5HZZ9
-
3,9-dichloro-6-(5,7-dichloro-9H-fluoren-2-yl)-5H-dibenzo[c,e]azepine-5,7(6H)-dione
-
68.9% inhibition at 0.02 mM
3,9-dichloro-6-(9H-fluoren-2-yl)-5H-dibenzo[c,e]azepine-5,7(6H)-dione
-
48% inhibition at 0.02 mM
3-(2,20-bithiophen-5-yl)-2-(1H-benzo-imidazol-2-yl)acrylonitrile
-
-
3-(2,4-dichlorophenyl)-5-(4-fluorophenethoxy)-N-hydroxypentanamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-(4-fluoro-2-methoxyphenyl)-N5-hydroxypentanediamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-(4-fluorophenethyl)-N5-hydroxypentanediamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-hydroxy-N5-(4-methoxyphenethyl)pentanediamide
A5HZZ9
-
3-(2,4-dichlorophenyl)-N1-hydroxy-N5-(o-tolyl)pentanediamide
A5HZZ9
-
3-(3,6-dioxocyclohexa-1,4-dien-1-yl)propanoic acid
A5HZZ9
-
3-(4-(1H-imidazol-1-yl)phenyl)-2-(1H-benzoimidazol-2-yl)acrylonitrile
-
-
3-(4-chloro-2-methylphenyl)-N-hydroxypropanamide
-
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3-fluoro-2-(naphthalene-2-carbonyl)benzoic acid
-
43.9% inhibition at 0.02 mM
3-hydroxy-N'-[(E)-(2-hydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
-
3-hydroxy-N'-[(E)-(3,4,5-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
competitive inhibition
3-hydroxy-N'-[(E)-(3-hydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
-
3-hydroxy-N-phenylanthracene-2-carboxamide
-
70.1% inhibition at 0.02 mM
32-mer C-terminal peptide of LcA
-
the activity of the light chain of botulinum toxin A is significantly reduced to 15% by the peptide with sequence KNFTGLFEFYKLLCVRGIITSKTKSLDKGYNK
-
4,4'-dichloro-2'-((9H -fluoren-2-ylamino)carbonyl)[1,1'-biphenyl]-2-carboxylic acid
-
88.3% inhibition at 0.02 mM
4,4'-dichloro-2'-[(5,7-dichloro-9H-fluoren-2-yl)carbamoyl][1,1'-biphenyl]-2-carboxylic acid
-
79.11% inhibition at 0.02 mM
4-(2-amino-3-sulfanylpropyl)benzamide
-
-
4-(2-amino-3-sulfanylpropyl)benzenesulfonamide
-
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4-(2-amino-3-sulfanylpropyl)benzenesulfonic acid
-
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4-amino-7-chloroquinoline
-
12% inhibition at 0.05 mM
4-chloro-(3-fluorophenyl)methyl benzenesulfonamide
-
i.e. MSU84, competitive inhibitor of botulinum neurotoxin type A light chain
4-chloro-N-[(4-fluorophenyl)methyl] pyridin-3-amine
-
i.e. MSU58, competitive inhibitor of botulinum neurotoxin type A light chain
4-chlorocinnamic hydroxamate
4-[((2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2R)-2-phenylethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl)]benzoic acid
-
-
4-[((2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(4-hydroxyphenyl)ethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl)]benzoic acid
-
-
4-[((2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl)]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(3H-imidazol-4-yl)ethylcarbamoyl]-(2S)-2-biphenyl-4-ylethylcarbamoyl)-3(S)sulfanylpropyl]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-methylbutylcarbamoyl)-(2S)-2-biphenyl-4-ylethylcarbamoyl]-3(S)-sulfanylpropyl]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2R)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl]benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1-methyl-1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-naphthalen-1-yl-ethylcarbamoyl]-3(S)sulfanylpropyl] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl]-3(S)sulfanylpropyl)] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(2S)-2-benzol[beta]thiophen-3-yl-1-benzylcarbamoylethylcarbamoyl-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3-(S)-sulfanylpropyl] benzoic acid
-
-
4-[(2S)-2-amino-3-[1-(2S)-2-benzo[b]thiophen-3-yl-1-benzylcarbamoylethylcarbamoyl-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)-sulfanylpropyl]benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2R)-2-phenylethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(3H-imidazol-4-yl)ethylcarbamoyl]-(2S)-2-biphenyl-4-yl-ethylcarbamoyl}-3(S)sulfanylpropyl)}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-(4-hydroxyphenyl)ethylcarbamoyl)-(2S)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2R)-2-biphenyl-4-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1-methyl-1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-(1H-indol-3-yl)ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl)-(2S)-2-naphthalen-1-yl-ethylcarbamoyl]-3(S)sulfanylpropyl}benzoic acid
-
-
4-{(2S)-2-amino-3-[1-(1-benzylcarbamoyl-(2S)-2-phenylethylcarbamoyl]-3(S)-sulfanylpropyl)}benzoic acid
-
-
5,8-dihydroxynaphthalene-1,4-dione
A5HZZ9
-
5,8-dioxo-5,8-dihydronaphthalen-1-yl acetate
A5HZZ9
-
5,8-dioxo-5,8-dihydronaphthalen-1-yl cyclopentanecarboxylate
A5HZZ9
-
5-((3-bromoadamantan-1-yl)methoxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
A5HZZ9
-
5-(allyloxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
A5HZZ9
-
5-(benzyloxy)-3-(2,4-dichlorophenyl)-N-hydroxypentanamide
A5HZZ9
-
5-(benzyloxy)naphthalene-1,4-dione
A5HZZ9
-
5-chloro-7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
5-chloro-7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
5-hydroxynaphthalene-1,4-dione
A5HZZ9
-
5-methoxynaphthalene-1,4-dione
A5HZZ9
-
5-methyl-2-(propan-2-yl)naphthalene-1,4-dione
A5HZZ9
-
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy)phenyl)-1H-benzo[d]imidazole
-
-
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy)phenyl)-1H-indole
-
-
6-(1,4,5,6-tetrahydropyrimidin-2-yl)-2-{5-[4-(1,4,5,6-tetrahydropyrimidin-2-yl)phenoxy]pyridin-2-yl}-1H-indole
-
-
6-(3,4,5,6-tetrahydropyrimidin-2-yl)-2-(4-(3,4,5,6-tetrahydropyrimidin-2-yl)phenyl)-1H-indole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4,5-dihydro-1H-imidazol-2-yl)phenyl)-1H-indole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)phenyl)-1H-benzo[d]imidazole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)phenyl)-1H-indole
-
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-(4-fluorophenyl)-1H-indole
-
-
6-(4,5-dihydroimidazol-2-yl)-2-(5-(4-(4,5-dihydroimidazol-2-yl)phenoxy)pyridine-2-yl)indole
-
-
6-(9H-fluoren-2-yl)-3,9-dinitro-5H-dibenzo[c,e]azepine-5,7(6H)-dione
-
24.7% inhibition at 0.02 mM
6-bromo-N-hydroxynaphthalene-2-carboxamide
-
-
6-chloro-2-(4-(4-(4,5-dihydro-1H-imidazol-2-yl)phenoxy)-phenyl)-1H-indole
-
-
6-chloro-N-hydroxy-1-benzothiophene-2-carboxamide
-
-
6-chloro-N-hydroxy-1-methyl-1H-indole-2-carboxamide
-
-
6-chloro-N-hydroxy-1H-indene-2-carboxamide
-
-
6-chloro-N-hydroxynaphthalene-2-carboxamide
-
-
6-hydroxynaphthalene-1,4-dione
A5HZZ9
-
6-[(2,5-dimethoxyphenyl)amino]-N-(4-phenoxybenzyl)picolinamide
A5HZZ9
-
6-[(3,6-dioxocyclohexa-1,4-dien-1-yl)amino]-N-(4-phenoxybenzyl)picolinamide
A5HZZ9
-
7-((4-nitroanilino)(phenyl)methyl)-8-quinolinol
-
NSC 1010
7-N-phenylcarbamoylamino-4-chloro-3-propyloxyisocoumarin
-
ICD 1578
7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2,4-difluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(2-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]-2-methylquinolin-8-ol
-
-
7-[(4-fluorophenyl)[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[phenyl[(pyridin-2-yl)amino]methyl]quinolin-8-ol
-
-
7-[phenyl[(pyridin-3-yl)amino]methyl]quinolin-8-ol
-
-
7-[phenyl[(pyrimidin-2-yl)amino]methyl]quinolin-8-ol
-
-
9H-fluorene
-
17.3% inhibition at 0.02 mM
Ac-SNKTRIDEACQRATKML-NH2
-
-
Ac-SNKTRIDEAN(D)CRATKML-NH2
-
-
Ac-SNKTRIDEAN(D)QCRATKML-NH2
-
-
Ac-SNKTRIDEANCRATKML-NH2
-
-
Ac-SNKTRIDEANQCATKML-NH2
-
-
Ala-Ser-Gln-Phe-Glu-Thr-Ser
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica, serotype BoNT/B, not A or E
aminopterin
P10845
11% inhibition at 0.01 mM
amodiaquine
-
antimalarial drug, 30% inhibition
antibody F1-40
-
F1-40 binds a peptide fragment of the BoNT/A light chain, designated L1-3, which spans from T125 to L200, with recognition motif QPDRS. No binding to BoNT/A mutant Q138G/P139G/D140G. Wild-type residues Q138, P139 and D140 form a loop on the external surface of BoNT/A, exposed to solvent
-
AQVDEVVDIMRVNVDKVLERDQ
-
residues 37-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
bis-aminoquinoline
P10845
60% inhibition at 0.02 mM
bisquinoline Q2-15
-
60% inhibition
bisquinoline Q2-61
-
50% inhibition
buforin I
-
natural peptide, isolated from the stomach of the Asian toad Bufo bufo gargarizans
-
CB 7969312
-
the quinolinol-based analogue effectively neutralizes BoNT/A toxicity, ex vivo protection at 500 nM
CB7967495
-
inhibitor of botulinum neurotoxin serotypes B, C, E, and F
CB7969312
-
inhibitor of botulinum neurotoxin serotypes B, C, E, and F
chicoric acid iso-propyl ester
A5HZZ9
competitive partial inhibition
Chloroquinone
P10845
7% inhibition at 0.02 mM
cinnamic acid hydroxamate
-
-
CpA
-
i.e. [5-(4-chlorobenzoyl)-2-phenylthiophen-3-yl]acetic acid, 15% inhibition of BoNTA at 0.1 mM
CRATKML
-
competitive peptide inhibitor
cyclohexa-2,5-diene-1,4-dione
A5HZZ9
-
D-chicoric acid
-
mechanism of inhibition, overview. The inhibitor binds to an exosite, displays noncompetitive partial inhibition, and is synergistic with a competitive inhibitor I2 when used in combination
desmosine
P10845
25% inhibition at 0.01 mM
Dyngo-4a
A5HZZ9
endocytic inhibitor of BoNT/A neurotoxicity through dynamin inhibition, competitive inhibition. Complete inhibition of the BoNT/A light chain at 0.02 mM
expoxomicin
-
increases ubiquitination of BoNT/B light chain in neuronal cells. Ubiquitination in vitro and in cells decreases the biological activity of BoNT/B light chain
ganglioside GT1b glycoconjugate
GGPPAPPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 17-58 of vesicle-associated membrane protein VAMP
Gln-Phe-Glu-Thr
-
synthetic peptide containing cleavage site of synaptobrevin, inhibits toxin action on buccal ganglion of Aplysia californica, serotype BoNT/B, not A or E
GRKKRRQRRRPPQC
-
90% inhibition
LQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 32-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
mefloquine
P10845
28% inhibition at 0.02 mM
methyl 3alpha-(N-[(7-chloroquinolin-4-yl)amino]ethyl)amino,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
-
-
methyl 3alpha-(N-[(7-chloroquinolin-4-yl)amino]ethyl)oxy,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
-
9% inhibition at 0.05 mM
methyl 3alpha-amino-7alpha,12alpha-diacetoxycholan-24-oate
-
13% inhibition at 0.05 mM
methyl 3beta-(N-[(7-chloroquinolin-4-yl)amino]ethyl)amino,7alpha,12alpha-diacetoxy-5beta-cholan-24-oate
-
-
methyl 6-[(3,6-dioxocyclohexa-1,4-dien-1-yl)amino]picolinate
A5HZZ9
-
methylamine hydrochloride
monensin
P10845
38% inhibition at 0.01 mM
N'-(2-(dimethylamino)ethyl)-2-(4-(4-(N'-2-(dimethylaminoethyl)carbamimidoyl)phenoxy)phenyl)-1H-indole-6-carboximidamide
-
-
N'-[(E)-(2,4,5-trihydroxyphenyl)methylidene]benzohydrazide
A5HZZ9
-
N'-[(E)-(2,4,5-trihydroxyphenyl)methylidene]naphthalene-2-carbohydrazide
A5HZZ9
-
N,N-bis(7-aminoheptyl)-1-benzyl-4-[3-(hydroxyamino)-3-oxopropyl]-5-(3-hydroxy-3,3-diphenylpropyl)-1H-pyrrole-2-carboxamide
-
a tetrasubstituted pyrrole inhibitor
N-(2,6-dimethylphenyl)-2-(pyridine-4-carbonyl)hydrazine-1-carbothioamide
-
28% inhibition at 0.02 mM
N-(2-chlorophenyl)-2-(pyridine-4-carbonyl)hydrazine-1-carbothioamide
-
19% inhibition at 0.02 mM
N-(3-amino-9H-fluoren-2-yl)acetamide
-
13.7% inhibition at 0.02 mM
N-(3alpha,7alpha,12alpha-triacetoxy-5beta-cholan-24-yl)-N'-(7'-chloroquinolin-4'-yl)-ethane-1,2-diamine
-
-
N-(4-bromobenzyl)-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
69% inhibition at 0.02 mM
N-(4-bromobenzyl)-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
68% inhibition at 0.02 mM
N-(4-phenoxybenzyl)picolinamide
A5HZZ9
-
N-(4-tert-butylbenzyl)-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
47% inhibition at 0.02 mM
N-(4-tert-butylbenzyl)-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
50.28% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-fluorobenzyl)ethane-1,2-diamine
P10845
68% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-fluorobenzyl)propane-1,3-diamine
P10845
50.09% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-methoxybenzyl)ethane-1,2-diamine
P10845
18% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(4-methoxybenzyl)propane-1,3-diamine
P10845
14% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-3-ylmethyl)ethane-1,2-diamine
P10845
25% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-3-ylmethyl)propane-1,3-diamine
P10845
39.89% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-4-ylmethyl)ethane-1,2-diamine
P10845
24% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-(pyridin-4-ylmethyl)propane-1,3-diamine
P10845
42.29% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-adamantylethane-1,2-diamine
P10845
51.4% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-[(4-methoxypyridin-3-yl)methyl]ethane-1,2-diamine
P10845
19% inhibition at 0.02 mM
N-(7-chloroquinolin-4-yl)-N'-[(4-methoxypyridin-3-yl)methyl]propane-1,3-diamine
P10845
43.25% inhibition at 0.02 mM
N-(9-oxo-9H-fluoren-2-yl)benzamide
-
12.7% inhibition at 0.02 mM
N-(methyl 7alpha,12alpha-diacetoxy-5beta-cholan-24-oate,3alpha-yloxy)-ethyl-N'-(7-chloroquinolin-4-yl)-ethane-1,2-diamine
-
62% inhibition at 0.05 mM
N-(pyridin-2-yl)prop-2-enamide
A5HZZ9
-
N-(pyridin-3-yl)prop-2-enamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-1-(2,5-dimethoxybenzyl)-1H-1,2,4-triazole-3-carboxamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-1-[(3,6-dioxocyclohexa-1,4-dien-1-yl)methyl]-1H-1,2,4-triazole-3-carboxamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-1H-1,2,4-triazole-3-carboxamide
A5HZZ9
-
N-([1,1'-biphenyl]-4-ylmethyl)-2-aminoacetamide
A5HZZ9
-
N-Ac-CRATKML
P10845
an inhibitory peptide, structure of the serotype A toxin light chain with an inhibitory peptide bound at the catalytic Zn(II) ion, the peptide is bound with the Cys Sgamma atom coordinating the metal ion, overview
N-acetyl neuraminic acid
-
both binding and permeation of toxins are potently inhibited by N-acetyl neuraminic acid in the cell culture mediumor by treatment of the cells with neuraminidase, but neither galactose, lactose nor N-acetyl galactosamine inhibit binding or permeation of toxins
N-acetyl-CRATKML-amide
-
-
N-benzyl-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
52% inhibition at 0.02 mM
N-benzyl-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
51.83% inhibition at 0.02 mM
N-hydroxy-2-(tricyclo[3.3.1.13,7]dec-1-yl)acetamide
A5HZZ9
-
N-hydroxy-4-pentylbenzamide
-
-
N-hydroxyacetamidoadamantan
-
a synthetic hydroxamate
N-[(4-chloropyridin-3-yl)methyl]-N'-(7-chloroquinolin-4-yl)ethane-1,2-diamine
P10845
23% inhibition at 0.02 mM
N-[(4-chloropyridin-3-yl)methyl]-N'-(7-chloroquinolin-4-yl)propane-1,3-diamine
P10845
35.87% inhibition at 0.02 mM
N-[3-(benzyloxy)phenyl]-2-[(2,5-dimethoxybenzyl)amino]acetamide
A5HZZ9
-
N-[3-(benzyloxy)phenyl]-2-[[(3,6-dioxocyclohexa-1,4-dien-1-yl)methyl]amino]acetamide
A5HZZ9
-
N1-(2-cyclopropylethyl)-3-(2,4-dichlorophenyl)-N5-hydroxypentanediamide
A5HZZ9
-
N1-(4-bromophenyl)-3-(2,4-dichlorophenyl)-N5-hydroxypentanediamide
A5HZZ9
-
N1-(6-(6-(4,5-dihydro-1H-imidazol-2-yl)benzo[b]thiophen-2-yl)-pyridine-3-yl)ethane-1,2-diamine
-
-
N1-(7-chloroquinolin-4-yl)-ethane-1,2-diamine
-
33% inhibition at 0.05 mM
N1-(7-chloroquinolin-4-yl)-propane-1,3-diamine
-
22% inhibition at 0.05 mM
naphthalene-1,4-dione
A5HZZ9
-
NSC 119889
-
56% inhibition
NSC 130796
-
48% inhibition
NSC 240898
-
NSC 240898, a potent BoNT/A LC endopeptidase inhibitor, 75% inhibition at 0.02 mM, no cytotoxicity
NSC 357756
-
57% inhibition
NSC 402959
-
40% inhibition
NSC 625324 (silver sulfadiazine)
-
100% inhibition
NSC 661755 (michellamine B)
-
62% inhibition
NSC 86372
-
51% inhibition
paclitaxel
P10845
95% inhibition at 0.01 mM
phorbol 12-myristate 13-acetate
-
increases ubiquitination of BoNT/B light chain in neuronal cells. Ubiquitination in vitro and in cells decreases the biological activity of BoNT/B light chain
PPPNLTSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 22-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
PTEN
P10845
a zinc-chelating agent
-
Quinacrine
-
antimalarial drug, 30% inhibition
RRGF
-
0.02 mM, 95% inhibition
S132B-C11
-
a RNA aptamer that inhibits the enzyme's endopeptidase activity in a non-competitive manner. The core sequence is GACAGCGUGCCUAGAAGUCCAAGCUUAAAUAACCACGCUCGACAAGC, structure, overview
-
S132B-C12
-
a RNA aptamer that inhibits the enzyme's endopeptidase activity in a non-competitive manner. The core sequence is ACAACCCGGAACAACGUCUAACAGUGUACCAUAACCCGGCAUUCA, structure, overview
-
S132B-C22
-
a RNA aptamer that inhibits the enzyme's endopeptidase activity in a non-competitive manner. The core sequence is AUUCGGGCCCAGGAACCAACUAUAUAAAUGUCCCGAAUGCUUCGACG, structure, overview
-
single-domain llama antibody Aa1
-
most potent antibody isolated from a single domain VHH, i.e. camelid heavy-chain variable region derived from heavy-chain-only antibody, antibodies, it is resistant to heat denaturation and reducing conditions. The Aa1 paratope coincides with an alpha-helical portion of the SNAP25 substrate. Structure of BoNT/A Lc-Aa1 VHH complex and inhibition mechanism, overview
-
synaptotagmin II luminal domain
-
the luminal domain of syt II, syt II-LD, inhibits the toxicity of BoNT/B by interfering with the toxin-receptor interaction. It contains toxin-binding sites that have a high affinity for BoNT/B heavy chain. Recombinant syt II-LD in vivo provides protection against BoNT/B intoxication in mice models to about 30% survivals at 0.27 mg/ml of sytII-LD, the neutralization effect is improved by using gangliosides to 60% survivals. Syt II-LD specifically binds to BoNT/B compared to other BoNT serotypes, overview
-
THF-toosendanin
-
tetrahydrofuran analogue of toosendanin, selectively arrests the light chain translocation step of intoxication with subnanomolar potency, and increases the unoccluded heavy chain channel propensity to open with micromolar efficacy, inhibitory profile on light chain translocation, overview. The bimodal modulation by toosendanin depends on the dynamic interactions between channel and cargo, highlighting their tight interplay during the progression of LC transit across endosomes
tris-(2-carboxyethyl)-phosphine hydrochloride
-
i.e. TCEP, a non-odorous, oxygen-insensitive, non-toxic sulfhydryl reducing compound, reduces proteolytic activity of BoNT/B in human neuronal SHSY-5Y cells at higher concentrations above 4 mM, protects against BoNT/B inhibition of noradrenaline release, achieving 72% of the release from un-intoxicated controls. TCEP significantly changes the conformation of BoNT/B holotoxin. But TCEP does not fragment un-nicked BoNT/B holotoxin
tris[3-(7-chloroquinolin-4-yl)aminopropyl]amine
-
-
Triticum vulgaris lectin
-
a known competitive antagonist of BoNT, inhibits the activation of neurit outgrowth by BoNT/A
-
TSNRRLQQTQAQVDEVVDIMRVNVDKVLERDQ
-
residues 27-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
VAMP 22-58/Gln58D-cysteine
a substrate-based inhibitor, that binds to BoNT F in the canonical direction but is positioned specifically via three major exosites away from the active site
-
VAMP 27-58/Gln58D-cysteine
a substrate-based inhibitor, that binds to BoNT F in the canonical direction but is positioned specifically via three major exosites away from the active site. The cysteine sulfur of the inhibitors interacts with the zinc and exists as sulfinic acid
-
VVDIMRVNVDKVLERDQ
-
residues 42-58 of vesicle-associated membrane protein VAMP. Inhibitor exhibits a high degree of specificity for BoNT F, compared to other BoNT serotypes
Zn2+
-
addition of exogenous ZnCl2 to the assay mixture reduces the activity of BoNT/Am activity ratio of wild-type and mutant enzymes in presence or absence of ZnCl2, overview
[[(5-[[1-(4-ammoniobutyl)-2-phenyl-1H-indol-6-yl]carbonyl]-2-phenylthiophen-3-yl)acetyl]amino]oxidanide
-
synthesis and binding structure, overview, multiple molecular dynamics simulations of the endopeptidase in complex with inhibitor 1 using the dummy atom approach, overview
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
-
a synthetic hydroxamate, D-chicoric acid is synergistic with a competitive inhibitor I2 when used in combination
(2E)-3-(2,4-dichlorophenyl)-N-hydroxyprop-2-enamide
-
-
1,10-phenanthroline
-
-
1,10-phenanthroline
-
r, Zn2+ restores
4-chlorocinnamic hydroxamate
-
-
4-chlorocinnamic hydroxamate
-
binding site and complex structure, overview
ammonium chloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
ammonium chloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
ammonium chloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
bafilomycin A1
-
inhibits all BoNT serotypes. The ATPase inhibitor also functions as antagonist of the acidification process
bafilomycin A1
-
inhibits all BoNT serotypes. The ATPase inhibitor also functions as antagonist of the acidification process
bafilomycin A1
-
inhibits all BoNT serotypes. The ATPase inhibitor also functions as antagonist of the acidification process
captopril
-
-
captopril
-
serotype BoNT/B
Chloroquine
-
antimalarial drug, 20% inhibition
Chloroquine
-
the C2II channel can be blocked by chloroquine and related compounds
concanamycin A
-
the ATPase inhibitor also functions as antagonist of the acidification process
concanamycin A
-
the ATPase inhibitor also functions as antagonist of the acidification process
concanamycin A
-
the ATPase inhibitor also functions as antagonist of the acidification process
EDTA
-
serotype BoNT/B
ganglioside GT1b glycoconjugate
-
the synthetic glycoconjugates based on GT1b prevents SNAP-25 cleavage in spinal cord cells of rat embryos
ganglioside GT1b glycoconjugate
-
the synthetic glycoconjugates based on GT1b prevents SNAP25 cleavage in spinal cord cells of rat embryos
ganglioside GT1b glycoconjugate
-
the synthetic glycoconjugates based on GT1b prevents SNAP25 cleavage in spinal cord cells of rat embryos
L-Arginine hydroxamate
-
binding site and complex structure, overview
L-Arginine hydroxamate
-
-
methylamine hydrochloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
methylamine hydrochloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
methylamine hydrochloride
-
affects the acidification step, acts to inhibit by neutralizing the endosomal pH and show antagonism against BoNT-induced paralysis
RRGC
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGC
-
0.02 mM, 95% inhibition, most potent inhibitor. When assayed in the presence of dithiothreitol, the inhibitory effect is drastically reduced
RRGI
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGI
-
0.02 mM, 90% inhibition
RRGL
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGL
-
0.02 mM, 95% inhibition
RRGM
P10845
an inhibitory substrate analogue tetrapeptide, binding structure, overview
RRGM
-
0.02 mM, 90% inhibition
toosendanin
-
i.e. TSDN, selectively arrests the light chain translocation step of intoxication with subnanomolar potency, and increases the unoccluded heavy chain channel propensity to open with micromolar efficacy, inhibitory profile on light chain translocation, overview. The bimodal modulation by toosendanin depends on the dynamic interactions between channel and cargo, highlighting their tight interplay during the progression of LC transit across endosomes. Toosendanin modulates both cargo-dependent and cargo-free activities of the BoNT/E protein-conducting channel
toosendanin
an enzyme translocation inhibitor that hinders subtype BoNT/B oligomerization
additional information
-
evaluation of relevant and available in vitro cell-based assays and in vivo assays for drug discovery and development, especially with regard to the potential for medium- to high-throughput automation and its use in identifying physiologically relevant inhibitors. BoNT intoxication steps as targets for inhibitors, schematic overview. Because all BoNT serotypes require the acidification step for inducing muscle failure, developing pan inhibitors that target this stage is an attractive approach. The cell entry of the toxin is inhibited by plant and animal lectines, glycoconjugates, and antibodies. The SNARE cleavage is inhibited by small molecule, peptide, and peptidomimetic inhibitors
-
additional information
-
less than 10% inhibition with captopril
-
additional information
-
inhibitory potency and activity-structure relationship of 4-amino-7-chloroquinoline substructure-based compounds, molecular modeling, overview, no inhibition by methyl cholate triacetate
-
additional information
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inhibitor virtual screening performed by computationally docking compounds of the NCI database into the active site of BoNT/A light chain, inhibition studies in neuroblastoma N2a cell-based and tissue-based mouse phrenic nerve hemidiaphragm assays, overview. Five quinolinol-based analogues effectively neutralize BoNT/A toxicity, with CB 7969312 exhibiting ex vivo protection at 500 nM
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identification of three RNA aptamers from a ssDNA random library through SELEX-process, which bind strongly to the light chain of type A BoNT and inhibit the endopeptidase activity, with IC50 in low nM range. Inhibition kinetic studies reveal low nM KI and non-competitive nature of their inhibition, enzyme docking study, and inhibition kinetics, overview
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monoclonal antibodies F1-2 and F1-40 do not inhibit the catalytic activity of BoNT/A, but inhibit the entry of the toxin into host neuronal cells, leading to reduced toxicity to mice, and block intracellular SNAP25 cleavage, overview
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analysis of Echinacea components in inhibition of BoNT/A protease, overview
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P10845
construction of type A-specific monoclonal antibodies using antigene heavy chain antibody fragment VH/VHH from a nonimmune camel, primers specific to human VH gene segments, and recombinant expression in phagemid-transformed Escherichia coli. The selected antibodies inhibiting the endopeptidase activity of BoTxA light chain and of botulism in hosts in vivo. Molecular docking and interface binding of BoTxA/LC and antibody VHH17
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BoNT/B LC is processed for removal via the proteasome-dependent degradation pathway after ubiquitination in neuronal cells
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development of specific potent inhibitors of BoNT/A light chain, structure-activity relationship studies, overview
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construction of a non-immune llama single-domain library for display on the surface of Saccharomyces cerevisiae and identification of a single-domain llama antibody that potently inhibits the enzymatic activity of BoNT/A light chain by binding to the non-catalytic alpha-exosite binding region, overview
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the toxicity of the enzyme is reduced in absence of gangliosides
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capsaicin interacts with TRPV1 receptors, transient receptor potential proteins of the vanilloid subfamily, on motor nerve endings to reduce BoNT/A uptake into Neuro 2a cells via a Ca2+-dependent mechanism, but capsaicin fails to protect against the neuroparalytic effects of BoNT/A. Capsaicin protects muscle functions and electromygraphic activity from the incapacitating effects of BoNT/A. Capsazepine pretreatment antagonizes the protective effect of capsaicin on acetylcholine release at high frequencies
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inhibitor synthesis, overview
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inhibition of enzymatic activity of botulinum neurotoxins/A1, /A2, and /A3 by a panel of monoclonal anti-BoNT/A antibodies
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development and synthesis of small molecule inhibitors of BoNTA endopeptidase, that antagonize the extracellular or intracellular toxin, in vivo pharmacokinetics in mice, overview. Extended multiple molecular dynamics simulations of inhibitor-enzyme complex formations, overview
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development of llama single domain antibodies specific for the seven botulinum neurotoxin serotypes as heptaplex immunoreagents. A single llama is immunized with a cocktail of seven BoNT toxoids to generate a phage display library of single domain antibodies, sdAb, VHH or nanobodies, which are selected on live toxins. Several sdAb act as both captor and tracer for several toxin and toxin complexes suggesting sdAb can be used as architectural probes to indicate BoNT oligomerisation, cross reactivities, overview
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semisynthetic strategy to identify inhibitors based on toosendanin, a traditional Chinese medicine reported to protect from BoNT intoxication, overview. No inhibition by deacetylted toosendanin and by toosendanin ketone and lactone analogues
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regions on BoNT/B that bind to blocking antibodies, synaptotagmin, or gangliosides, recognition pattern, overview
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evaluation of relevant and available in vitro cell-based assays and in vivo assays for drug discovery and development, especially with regard to the potential for medium- to high-throughput automation and its use in identifying physiologically relevant inhibitors. BoNT intoxication steps as targets for inhibitors, schematic overview. Because all BoNT serotypes require the acidification step for inducing muscle failure, developing pan inhibitors that target this stage is an attractive approach. The cell entry of the toxin is inhibited by plant and animal lectines, glycoconjugates, and antibodies. The SNARE cleavage is inhibited by small molecule, peptide, and peptidomimetic inhibitors
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a tetrapeptide provides an optimum length as the most efficient peptide inhibitor that binds at the active site normally occupied by the substrate. The peptides survive within neurons for at least 40 h and inhibit BoNT/A activity within two primary neuronal cells without showing any apparent cellular toxicity
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the recombinant subtype A4 neurotoxin is effectively neutralized by botulism heptavalent antitoxin
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peptide HN729-845(corresponding to the BoNT/A region comprising heavy-chain N-terminal domain residues 729 to 845) is able to inhibit the binding of 125I-labeled serotype BoNT/A to synaptosomes
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the C-terminal peptides of LcB-1, LcC1-1, LcD-1, and LcF-1 show no inhibitory effect
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P10845
not inhibited by D-fructose
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P10845
not inhibited by artemisin
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the receptor-binding domain of botulinum neurotoxin serotype B significantly delays intoxication by botulinum neurotoxin serotype B
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additional information
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evaluation of relevant and available in vitro cell-based assays and in vivo assays for drug discovery and development, especially with regard to the potential for medium- to high-throughput automation and its use in identifying physiologically relevant inhibitors. BoNT intoxication steps as targets for inhibitors, schematic overview. Because all BoNT serotypes require the acidification step for inducing muscle failure, developing pan inhibitors that target this stage is an attractive approach. The cell entry of the toxin is inhibited by plant and animal lectines, glycoconjugates, and antibodies. The SNARE cleavage is inhibited by small molecule, peptide, and peptidomimetic inhibitors
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