Inhibition of the protease activity of the light chain of type A botulinum neurotoxin by aqueous extract from stinging nettle (Urtica dioica) leaf.
We investigated the inhibitory effect of stinging nettle leaf extract on the protease activity of botulinum neurotoxin type A and B light chains. The nettle leaf infusion was fractionated and HPLC-based enzymatic assays were performed to determine the capacity of each fraction to inhibit the protease activity of botulinum neurotoxin type A and B light chains. Assay results demonstrated that a water-soluble fraction obtained from the nettle leaf infusion inhibited type A, but did not inhibit type B light chain protease activity. The inhibition mode of water soluble fraction against protease activity of type A light chain was analyzed and found to be a non-competitive.
Gul
Nizamettin
N
Department of Immunology and Molecular Biology, Division of Toxinology and Aerobiology, U.S. Army Medical Research Institute of Infectious Diseases, 1425 Porter Street, Fort Detrick, MD 21702-5011, USA. nizamettin.gul@det.amedd.army.mil
Ahmed
S Ashraf
SA
Smith
Leonard A
LA
D019274:Botulinum Toxins, Type A / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D010936:Plant Extracts / Q000494:pharmacology; D018515:Plant Leaves / Q000737:chemistry; D011480:Protease Inhibitors / Q000494:pharmacology*; D026982:Urtica dioica / Q000737:chemistry*
D010936:Plant Extracts; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D019274:Botulinum Toxins, Type A