The relaxin peptide family - structure, function and clinical applications

LJ Chan; MA Hossain; CS Samuel; F Separovic; JD Wade

Journal article

The relaxin peptide family - structure, function and clinical applications

LJ Chan, MA Hossain, CS Samuel, F Separovic, JD Wade

Protein and Peptide Letters | BENTHAM SCIENCE PUBL LTD | Published : 2011

DOI: 10.2174/092986611794578396

Abstract

The relaxin peptide family in humans consists of seven members, relaxin-1, -2 and -3 and insulin-like (INSL) peptides 3, 4, 5 and 6. It is an offshoot of the large insulin superfamily. Each member consists of two chains, commonly referred to as A and B, which are held together by two inter-chain disulfide bonds and another intra-chain disulfide bond present within the A chain. The cysteine residues present in each chain, together with the distinctive disulfide bonding pattern, are conserved across all members of the superfamily. The chemical synthesis of these complex peptides poses a significant challenge. In the past, random combination of the two synthetic S-reduced chains under oxidizing..

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University of Melbourne Researchers

Akhter Hossain Author

Frances Separovic Author

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Grants

Awarded by NHMRC

Funding Acknowledgements

LJC is the recipient of a Faculty of Science, University of Melbourne, Postgraduate Research Scholarship, MAH is the recipient of a John T. Reid Charitable Trusts Fellowship, CSS is the recipient of a National Heart Foundation of Australia / NHMRC RD Wright Fellowship and JDW is the recipient of the NHMRC Principal Research Fellowship. Several of the recent studies reported in this review were funded by NHMRC Project grants 508995 and 509048 to JDW. We thank Professor Geoffrey Tregear, Howard Florey Institute, for his long-standing support.