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Controlling the helical screw sense of peptides with C ‐terminal L‐valine
Author(s) -
Demizu Yosuke,
Yamagata Nanako,
Sato Yukiko,
Doi Mitsunobu,
Tanaka Masakazu,
Okuda Haruhiro,
Kurihara Masaaki
Publication year - 2010
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1213
Subject(s) - pentapeptide repeat , valine , stereochemistry , chemistry , peptide , aminoisobutyric acid , crystallography , amino acid residue , amino acid , peptide sequence , biochemistry , gene
One chiral L ‐valine ( L ‐Val) was inserted into the C ‐terminal position of achiral peptide segments constructed from α‐aminoisobutyric acid (Aib) and α,β‐dehydrophenylalanine (Δ Z Phe) residues. The IR, 1 H NMR and CD spectra indicated that the dominant conformations of the pentapeptide Boc‐Aib‐ΔPhe‐(Aib) 2 ‐ L ‐Val‐NH‐Bn (3) and the hexapeptide Boc‐Aib‐ΔPhe‐(Aib) 3 ‐ L ‐Val‐NH‐Bn (4) in solution were both right‐handed ( P ) 3 10 ‐helical structures. X‐ray crystallographic analyses of 3 and 4 revealed that only a right‐handed ( P ) 3 10 ‐helical structure was present in their crystalline states. The conformation of 4 was also studied by molecular‐mechanics calculations. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd.