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Structure-activity studies on prolactin-releasing peptide (PrRP). Analogues of PrRP-(19-31)-peptide

Authors :
Stuart Travers
Robert George Boyle
Tanmoy Ganguly
Jeff Smith
John Humphries
Robert Downham
Source :
Journal of Peptide Science. 11:161-165
Publication Year :
2005
Publisher :
Wiley, 2005.

Abstract

An investigation of a series of single replacement analogues of PrRP-(19–31)-peptide has shown that good functional activity was retained when Phe31 was replaced with His(Bzl), Phe(4Cl), Nle, Trp, Cys(Bzl) or Glu(OBzl); when Val28 or Ile25 was replaced with Phg; when Gly24 was replaced with D-Ala, L-Ala, Pro or Sar; when Ser22 was replaced with Gly and when Ala21 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-NH2. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.

Details

ISSN :
10991387 and 10752617
Volume :
11
Database :
OpenAIRE
Journal :
Journal of Peptide Science
Accession number :
edsair.doi.dedup.....aeb43ca3fe42a3c8bdb6bebfddc5ea4c
Full Text :
https://doi.org/10.1002/psc.612