Crystal structure analysis of helix-turn-helix type motifs in α,γ-hybrid peptides

Mimicking protein supersecondary structures using short synthetic peptide sequences holds significant importance in the fields of synthetic protein design, catalysis, and drug discovery. In this study, we present a series of helix-turn-helix motifs derived from short α,γ-hybrid peptides, incorporati...

Full description

Saved in:
Bibliographic Details
Published in:CrystEngComm 2024-02, Vol.26 (7), p.913-917
Main Authors: Nalawade, Sachin A, Kumar, Mothukuri Ganesh, Puneeth Kumar, DRGKoppalu R, Singh, Manjeet, Dey, Sanjit, Gopi, Hosahudya N
Format: Article
Language:English
Subjects:
Amino acids
Crystal structure
Helices
Peptides
Proteins
Residues
Sequences
Structural analysis
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mimicking protein supersecondary structures using short synthetic peptide sequences holds significant importance in the fields of synthetic protein design, catalysis, and drug discovery. In this study, we present a series of helix-turn-helix motifs derived from short α,γ-hybrid peptides, incorporating centrally positioned E -α,β-unsaturated γ-amino acids. By varying the number of trans double bonds at the central residue, the positioning of the helices can be adjusted. Superimposing the synthetic seven-residue helix-turn-helix motif with the natural calcium-binding helix-turn-helix motif revealed the potential to design three-dimensional helix-turn-helix motifs within short peptide sequences. Design of helix-turn-helix type mimetics using short α,γ-hybrid peptides as helices and ( E )-α,β-unsaturated γ-amino acids as conformationally rigid linkers and their conformations in single crystals are reported.
ISSN:1466-8033
1466-8033
DOI:10.1039/d3ce01236k