Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids

Abstract

In this article, we review the relevant results obtained during almost 60 years of research on a specific aspect of stereochemistry, namely handedness preference and switches between right-handed and left-handed helical peptide structures generated by protein amino acids or appropriately designed, side-chain modified analogs. In particular, we present and discuss here experimental and theoretical data on three categories of those screw-sense issues: (i) right-handed/left-handed α-helix transitions underwent by peptides rich in Asp, specific Asp β-esters, and Asn; (ii) comparison of the preferred conformations adopted by helical host-guest peptide series, each characterized by an amino acid residue (e.g. Ile or its diastereomer aIle) endowed with two chiral centers in its chemical structure; and (iii) right-handed (type I)/left-handed (type II) poly-(Pro)n helix transitions monitored for peptides rich in Pro itself or its analogs with a pyrrolidine ring substitution, particularly at the biologically important position 4. The unique modular and chiral properties of peptides, combined with their relatively easy synthesis, the chance to shape them into the desired conformation, and the enormous chemical diversity of their coded and non-coded α-amino acid building blocks, offer a huge opportunity to structural chemists for applications to bioscience and nanoscience problems.

Rapid Filament Supramolecular Chirality Reversal of HET-s (218–289) Prion Fibrils Driven by pH Elevation

“…Similar handedness inversion behavior in certain helical peptides in response to side-chain substitution as well as other external stimuli is well documented. 22 We also demonstrated that the observed changes in Trp fluorescence intensity are independent of changes in ionic strength associated with the pH elevation ( Figure S3, Supporting Information).…”

Parity Violation in Supramolecular Aggregation: Insights from Optoelectronic Properties

“…In biological context, chirality, and helicity constitute the fundamental aspects that regulate the selectivity and specificity of biomolecules such as proteins and DNA . Evolutionary, natural proteins are composed of homopolymer of L‐amino acids and fold into functional superstructures with preference to right‐handed helical conformation . Inspired by nature, transfer of chirality from monomeric chiral building block to supramolecular structure employing various non‐covalent interactions such as H‐bonding, π‐stacking, and hydrophobicity garner much interest due to their potential applications in chiral recognition and sensing, optical and electronic devices and biological systems .…”

Insights into the helix‐sense inversion of poly(β‐phenethyl‐L‐aspartate) by two‐dimensional Raman correlation spectroscopy

“…The helix‐sense inversion in surface‐grafted PPLA, PBLA, and blockcopolymer of PBLA was observed. Recently, the results obtained during almost 60 years of research on handedness preference and switches between right‐handed and left‐handed helical peptides including polyaspartates were reviewed …”