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Capping β‐hairpin with N‐terminal d ‐amino acid stabilizes peptide scaffold
Author(s) -
Makwana Kamlesh M.,
Mahalakshmi Radhakrishnan
Publication year - 2016
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22837
Subject(s) - chemistry , scaffold , peptide , terminal (telecommunication) , amino acid , hydrogen bond , scaffold protein , stereochemistry , combinatorial chemistry , biophysics , biochemistry , molecule , organic chemistry , medicine , telecommunications , signal transduction , computer science , biomedical engineering , biology
Various strategies exist to stabilize de novo designed synthetic peptide β‐hairpins or β‐sheets structures, especially at the non‐hydrogen bonding position. However, strategies to stabilize strand termini, which are affected by fraying, are highly limited. Here, by substituting N‐terminal aliphatic amino acid with its mirror image counterpart, we achieve a significant increase in scaffold stabilization, resulting from the formation of a terminal aliphatic–aromatic hydrophobic CH…pi cluster. Our extensive solution NMR studies support the incorporation of an N‐terminal d‐ aliphatic amino acid in the design of short β‐hairpins, while successfully retaining the overall structural scaffold. © 2016 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 106: 260–266, 2016.