Intramolecular CH⋯π attraction mediated conformational polymorphism of constrained helical peptides.

ABSTRACT: In nature, biochemical processes depend on polymorphism, a phenomenon by which discrete biomolecules can adopt specific conformations based on their environment. However, it is often difficult to explore the generation mechanism and achieve polymorphic control in artificial supramolecular assembly systems. In this work, we propose a feasible thought for exploring the transformation mechanism of polymorphism in peptide assembly from the perspective of thermodynamic regulation, which enables polymorphic composition to be limited by switchable intramolecular CH⋯π attraction within a certain temperature range. Combined with the density functional theory calculations, we obtained thermodynamic theoretical data supporting the conformation transition and the underlying polymorphism formation prin

SUBMITTER: Sun J 

PROVIDER: S-EPMC11322895 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature