Abstract
Conotoxins, disulfide-rich peptides derived from cone snails' venom, exhibit diverse biological activities and structural variations, leading to their classification into distinct subfamilies [1]. Each subfamily possesses the ability to target various pharmacological receptors, including nicotinic acetylcholine receptors (nAChRs), sodium channels, and G protein-coupled receptors, with additional receptor types yet to be explored. Despite their pharmacological significance, synthesizing these peptides presents a considerable challenge due to the presence of multiple disulfide bridges, numbering up to five or more. These bridges confer a unique three-dimensional structure to conotoxins, enhancing their affinity for the targeted receptors [2].The development of versatile chemical synthesis strategies for these compounds is crucial to unlocking their untapped potential. Through my communication, the discussion will focus on a comparison of the results obtained via aqueous oxidative folding (AOF), organic oxidative folding (OOF), and a one-pot fast regioselective folding (OpRF) of a three disulfide bonds conotoxin with a particular cysteine framework [1].References1. Akondi KB, Muttenthaler M, Dutertre S, Kaas Q, Craik DJ, Lewis RJ, Alewood PF. Discovery, Synthesis, and Structure–Activity Relationships of Conotoxins. Chem Rev. 2014; 114: 5,815-5,847. 10.1021/cr400401e.2. Góngora-Benítez M, Tulla-Puche J, Albericio F. Multifaceted Roles of Disulfide Bonds. Peptides as Therapeutics. Chem Rev. 2014; 114: 901-926. 10.1021/cr400031z.