Minimum active structure of insulin-like peptide 5

A Belgi; RAD Bathgate; M Kocan; N Patil; S Zhang; GW Tregear; JD Wade; MA Hossain

Journal article

Minimum active structure of insulin-like peptide 5

A Belgi, RAD Bathgate, M Kocan, N Patil, S Zhang, GW Tregear, JD Wade, MA Hossain

Journal of Medicinal Chemistry | AMER CHEMICAL SOC | Published : 2013

DOI: 10.1021/jm400924p

Abstract

Insulin-like peptide 5 (INSL5) is a complex two-chain peptide hormone constrained by three disulfide bonds in a pattern identical to insulin. High expression of INSL5 in the colon suggests roles in activation of colon motility and appetite control. A more recent study indicates it may have significant roles in the regulation of insulin secretion and β-cell homeostasis. This peptide thus has considerable potential for the treatment of eating disorders, obesity, and/or diabetes. However, the synthesis of INSL5 is extremely challenging either by chemical or recombinant means. The A-chain is very poorly soluble and the B-chain is highly aggregating in nature which, together, makes their postsynt..

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University of Melbourne Researchers

Ross Bathgate Author

Akhter Hossain Author

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Grants

Awarded by NHMRC (Australia)

Awarded by ARC

Awarded by Australian Research Council

Funding Acknowledgements

This research was partly funded by NHMRC (Australia) project grants (508995, 1023078, 1023321) and ARC linkage grant (LP120100654) to J.D.W., M.A.H., R.A.D.B., and R.A.H. We are grateful to Tania Ferraro and Sharon Layfield for assistance with biochemical assays and to Feng Lin for amino acid analysis. During these studies, M.A.H. was the recipient of Florey Foundation Fellowships. R.A.D.B. is an NHMRC Senior Research Fellow, and J.D.W. is an NHMRC Principal Research Fellow. Studies at the FINMH were supported by the Victorian Government's Operational Infrastructure Support Program.