Ambidextrous α,γ-Hybrid Peptide Foldamers

Rajkumar Misra, Gijo George, Abhijith Saseendran, Srinivasarao Raghothama, Hosahudya N. Gopi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)4408-4414
Number of pages7
JournalChemistry - An Asian Journal
Issue number23
StatePublished - 2 Dec 2019
Externally publishedYes


  • 3-helix
  • Schellman motif
  • achiral peptides
  • foldamers
  • tendril perversion


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