Impact of Dehydroamino Acids on the Structure and Stability of Incipient 3₁₀-Helical Peptides.

ABSTRACT: A comparative study of the impact of small, medium-sized, and bulky α,β-dehydroamino acids (ΔAAs) on the structure and stability of Balaram's incipient 3₁₀-helical peptide (1) is reported. Replacement of the N-terminal Aib residue of 1 with a ΔAA afforded peptides 2a-c that maintained the 3₁₀-helical shape of 1. In contrast, installation of a ΔAA in place of Aib-3 yielded peptides 3a-c that preferred a β-sheet-like conformation. The impact of the ΔAA on peptide structure was independent of size, with small (ΔAla), medium-sized (Z-ΔAbu), and bulky (ΔVal) ΔAAs exerting similar effects. The proteolytic stabilities of 1 and its analogs were determined by incubation with Pronase. Z-ΔAbu and ΔVal increase

SUBMITTER: Joaquin D 

PROVIDER: S-EPMC7077758 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature