Regioselective Disulfide Solid Phase Synthesis, Chemical Characterization and In Vitro Receptor Binding Activity of Equine Relaxin

• Published in: International journal of peptide research and therapeutics Vol. 12; no. 3; pp. 211 - 215
• Main Authors: Hossain, Mohammed Akhter, Lin, Feng, Zhang, Soude, Ferraro, Tania, Bathgate, Ross A., Tregear, Geoffrey W., Wade, John D.
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Nature B.V 01.09.2006
• Subjects: Peptides; Pregnancy
• ISSN: 1573-3149; 1573-3904
• DOI: 10.1007/s10989-006-9020-9

Issue Title: Australian Peptide Conference Issue In the equine industry, pregnancy loss during the third trimester constitutes a large percentage of fetal and neonatal mortality and represents a major financial loss and time investment for the breeder. Early identification of placental insufficiency would, in some cases, make it possible to sustain the pregnancy through medical intervention. Recent work suggests that relaxin is a valuable clinical tool for diagnosing placental insufficiency and monitoring treatment efficacy in mares. Relaxin is a polypeptide member of the insulin superfamily that consists of a two-chain structure and three disulfide bonds in a disposition identical to that of insulin. It is typically produced in the ovary during pregnancy and has primary roles in maintaining mammalian pregnancy and facilitating the delivery of the young via remodelling of the reproductive tract. The placenta is the primary source of relaxin in the mare during pregnancy. Its primary structure has been determined and shown to be the smallest of the known mammalian relaxins. It consists of a 20 residue A-chain and a 28-residue B-chain. To undertake detailed biophysical and biological characterization of the peptide, its chemical synthesis was undertaken using regioselective disulfide formation methods. The synthetic equine relaxin showed typical α-helical structure under physiological conditions. The peptide was found to bind to the relaxin receptor, LGR7, in vitro, and its binding affinity was found to be higher than that of the "gold standard", porcine relaxin, and similar to that of the human relaxin-2 (H2 relaxin).[PUBLICATION ABSTRACT]