Conformational Heterogeneity of Pro-Pro Containing 23-Membered Ring Conopeptides by NMR.

ABSTRACT: Conformational diversity in conopeptides, Be828 and Li833, for which sequences are identified from Conus betulinus and Conus lividus has been explored in the present study. Be828 and Li833 have 23-membered rings with two consecutive prolines at positions 2/3 and 4/5, respectively, an unusual phenomenon observed in contryphans. These peptides provided an excellent scope to probe distinct conformational states, i.e., cis-trans isomerization around Xaa-Pro and Pro-Pro bonds. NMR analysis revealed that Be828 exists as a single trans (C1-P2)/trans (P2-P3) conformation, whereas Li833 exists in four distinct conformers across the consecutive proline bonds. Studies on synthetic analogues disclosed that the conformational heterogeneity in Li833 is influenced by the const

SUBMITTER: Dhurjad P 

PROVIDER: S-EPMC12631695 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature