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Conformation of diastereomeric peptide sequences: Structural analysis of Z‐ D ‐Val‐Ac 6 c‐Gly‐ L ‐Phe‐OMe
Author(s) -
Di Blasio B.,
Lombardi A.,
Nastri F.,
Saviano M.,
Pedone C.,
Yamada T.,
Nakao M.,
Kuwata S.,
Pavone V.
Publication year - 1992
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.360320904
Subject(s) - tetrapeptide , chemistry , diastereomer , dipeptide , stereochemistry , peptide , amino acid , cyclic peptide , crystallography , biochemistry
We have recently undertaken a systematic structural analysis of fully protected tetrapeptides containing at the N‐ and C‐terminus either homo‐ or heterochiral amino acids, spaced by an achiral dipeptide segment. The interest for this class of peptides derives from the observation that, on reverse‐phase (HPLC), the homo‐ and heterochiral sequences have a markedly different retention times. The diastereomeric sequences, namely Z‐( L / D )‐Val‐X‐Y‐ L ‐Phe‐OMe (X = Sar, Gly, Ac 3 c, Aib, Ac 5 c, Ac 6 c, Deg, Dpg, Dbu, Dip, Dph; Y = Sar, Gly, Ac 3 c, Aib, Ac 6 c, Ac 6 c) show different overall hydrophobicity attributed to a different three‐dimensional structure that also depends on the X‐Y segment. Therefore, following preliminary studies in solution, we report here the detailed x‐ray analysis of the tetrapeptide Z‐ D ‐Val‐Ac 6 c‐Gly‐ L ‐Phe‐OMe in order to understand the structural features governing the overall hydrophobicity of linear fully protected tetrapeptides. © 1992 John Wiley & Sons, Inc.