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Ambidextrous α,γ‐Hybrid Peptide Foldamers
Author(s) -
Misra Rajkumar,
George Gijo,
Saseendran Abhijith,
Raghothama Srinivasarao,
Gopi Hosahudya N.
Publication year - 2019
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201901411
Subject(s) - helix (gastropod) , folding (dsp implementation) , monomer , chemistry , peptide , amino acid , stereochemistry , chirality (physics) , molecule , crystallography , biochemistry , polymer , organic chemistry , biology , physics , quantum mechanics , quark , snail , nambu–jona lasinio model , electrical engineering , engineering , ecology , chiral symmetry breaking
Molecular chirality is ubiquitous in nature. The natural biopolymers, proteins and DNA, preferred a right‐handed helical bias due to the inherent stereochemistry of the monomer building blocks. Here, we are reporting a rare co‐existence of left‐ and right‐handed helical conformations and helix‐terminating property at the C‐terminus within a single molecule of α,γ‐hybrid peptide foldamers composed of achiral Aib (α‐aminoisobutyric acid) and 3,3‐dimethyl‐substituted γ‐amino acid (Adb; 4‐amino‐3,3‐dimethylbutanoic acid). At the molecular level, the left‐ and right‐handed helical screw sense of α,γ‐hybrid peptides are representing a macroscopic tendril perversion. The pronounced helix‐terminating behaviour of C‐terminal Adb residues was further explored to design helix–Schellman loop mimetics and to study their conformations in solution and single crystals. The stereochemical constraints of dialkyl substitutions on γ‐amino acids showed a marked impact on the folding behaviour of α,γ‐hybrid peptides.