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Computationally designed β‐turn foldamers of γ‐peptides based on 2‐(aminomethyl)cyclohexanecarboxylic acid
Author(s) -
Kang, Young Kee,
Byun Byung Jin
Publication year - 2012
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22119
Subject(s) - chemistry , dipeptide , turn (biochemistry) , gramicidin , peptide , hydrogen bond , gramicidin s , peptidomimetic , cyclohexanecarboxylic acid , amino acid , planarity testing , stereochemistry , peptide bond , combinatorial chemistry , crystallography , molecule , organic chemistry , biochemistry , membrane
The γ‐peptide β‐turn structures have been designed computationally by the combination of chirospecific γ2, 3‐residues of 2‐(aminomethyl)cyclohexanecarboxylic acid (γAmc 6 ) with a cyclohexyl constraint on the C α −C β bond using density functional methods in water. The chirospecific γAmc 6 dipeptide with the (2S,3S)‐(2R,3R) configurations forms a stable turn structure in water, resembling a type II′ turn of α‐peptides, which can be used as a β‐turn motif in β‐hairpins of Ala‐based α‐peptides. The γAmc 6 dipeptide with homochiral (2S,3S)‐(2S,3S) configurations but different cyclohexyl puckerings shows the capability to be incorporated into one of two β‐turn motifs of gramicidin S. The overall structure of this gramicidin S analogue is quite similar to the native gramicidin S with the same patterns and geometries of hydrogen bonds. Our calculated results and the recently observed results may imply the wider applicability of chirospecific γ‐peptides with a cyclohexyl constraint on the backbone to form various peptide foldamers. © 2012 Wiley Periodicals, Inc. Biopolymers 97:1018–1025, 2012.