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Aim:To determine the structure factors that mediate the intoxication process ofbotulinum neurotoxin type A(BoNT/A).Methods:Triton X-114 phase separationexperiments and 1-anilino-8-naphthalene sulfonate binding assay were used tostudy the structural factor that corresponds to the hydrophobicity change ofBoNT/A.In addition,sucrose density gradient centrifugation and a chemicalcrosslinking study were employed to determine the quaternary structure of BoNT/A.Results:Our results demonstrated that in other than acidic conditions,thedisulfide reduction is the structural factor that corresponds to the hydrophobicitychange of BoNT/A.The quaternary structure of BoNT/A exists as a dimmer inacidic solution(pH 4.5),although the monomeric structure of BoNT/A was re-ported based on X-ray crystallography.Conclusion:Disulfide bond reduction iscritical for BoNT/A’s channel formation and ability to cross endosome membranes.This result implies that compounds that block this disulfide bond reduction mayserve as potential therapeutic agents for botulism.
Aim: To determine the structure factors that mediate the intoxication process of botulinum neurotoxin type A (BoNT / A). Methods: Triton X-114 phase separation experiments and 1-anilino-8-naphthalene sulfonate binding assay were used tostudy the structural factor that corresponds to the hydrophobicity change of BoNT / A. In addition, sucrose density gradient centrifugation and a chemical crosslinking study were employed to determine the quaternary structure of BoNT / A. Results: Our results for that in other than acidic conditions, thedisulfide reduction is the structural factor that the to the hydrophobicity of BoNT / A. The quaternary structure of BoNT / A exists as a dimmer in acid solution (pH 4.5), although the monomeric structure of BoNT / A was re-ported on X-ray crystallography. Conlusion: Disulfide bond reduction iscritical for BoNT / A’s channel formation and ability to cross endosome membranes. This result implies that compounds that block this disulfide bond reduction mayse rve as potential therapeutic agents for botulism.