Relaxin family peptides: structure–activity relationship studies. (19th January 2017)

• Record Type: Journal Article
• Authors: Patil, Nitin A; Rosengren, K Johan; Separovic, Frances; Wade, John D; Bathgate, Ross A D; Hossain, Mohammed Akhter
• Is Part Of: British journal of pharmacology. Volume 174:Number 10(2017)
• Page Start: 950
• Page End: 961
• Publication Date: 2017-01-19
• Subjects: Pharmacology -- Periodicals; Chemotherapy -- Periodicals; Drug Therapy -- Periodicals; Pharmacology -- Periodicals; 615.1
• DOI: 10.1111/bph.13684
• Languages: English
• ISSNs: 0007-1188

Abstract

Abstract : The human relaxin peptide family consists of seven cystine‐rich peptides, four of which are known to signal through relaxin family peptide receptors, RXFP1–4. As these peptides play a vital role physiologically and in various diseases, they are of considerable importance for drug discovery and development. Detailed structure–activity relationship (SAR) studies towards understanding the role of important residues in each of these peptides have been reported over the years and utilized for the design of antagonists and minimized agonist variants. This review summarizes the current knowledge of the SAR of human relaxin 2 (H2 relaxin), human relaxin 3 (H3 relaxin), human insulin‐like peptide 3 (INSL3) and human insulin‐like peptide 5 (INSL5). Linked Articles: This article is part of a themed section on Recent Progress in the Understanding of Relaxin Family Peptides and their Receptors. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v174.10/issuetoc