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Structure‐activity studies on prolactin‐releasing peptide (PrRP). Analogues of PrRP‐(19–31)‐peptide
Author(s) -
Boyle Robert G,
Downham Robert,
Ganguly Tanmoy,
Humphries John,
Smith Jeff,
Travers Stuart
Publication year - 2005
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.612
Subject(s) - peptide , chemistry , stereochemistry , prolactin , biochemistry , hormone
Abstract An investigation of a series of single replacement analogues of PrRP‐(19–31)‐peptide has shown that good functional activity was retained when Phe 31 was replaced with His(Bzl), Phe(4Cl), Nle, Trp, Cys(Bzl) or Glu(OBzl); when Val 28 or Ile 25 was replaced with Phg; when Gly 24 was replaced with D ‐Ala, L ‐Ala, Pro or Sar; when Ser 22 was replaced with Gly and when Ala 21 was replaced with Thr or MeAla. The results confirm that the functionally important residues are located within the carboxyl terminal segment, ‐Ile‐Arg‐Pro‐Val‐Gly‐Arg‐Phe‐NH 2 . Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.