Toxic Peptides from the Mexican Scorpion <i>Centruroides villegasi</i>: Chemical Structure and Evaluation of Recognition by Human Single-Chain Antibodies.

ABSTRACT: Alternative recombinant sources of antivenoms have been successfully generated. The application of such strategies requires the characterization of the venoms for the development of specific neutralizing molecules against the toxic components. Five toxic peptides to mammals from the Mexican scorpion Centruroides villegasi were isolated by chromatographic procedures by means of gel filtration on Sephadex G-50, followed by ion-exchange columns on carboxy-methyl-cellulose (CMC) resins and finally purified by high-performance chromatography (HPLC) columns. Their primary structures were determined by Edman degradation. They contain 66 amino acids and are maintained well packed by four disulfide bridges, with molecular mass from 7511.3 to 7750.1 Da. They are all relatively toxic and deadl

SUBMITTER: Riano-Umbarila L 

PROVIDER: S-EPMC11280942 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature