Effect of C‐Terminal Amidation on Folding and Disulfide‐Pairing of α‐Conotoxin ImI

Abstract

Building bridges: α-Conotoxins (C1–C3, C2–C4 disulfide pairing) adopt a globular conformation, whereas χ/λ-conotoxins (C1–C4, C2–C3 disulfide pairing) fold into a ribbon conformation. Amidation of the peptide C terminus has been shown to influence the folding (see picture) and hence the biological activity of conotoxins.