Journal article

Synthesis of fluorescent analogs of relaxin family peptides and their preliminary in vitro and in vivo characterization

Linda J Chan, Craig M Smith, Berenice E Chua, Feng Lin, Ross AD Bathgate, Frances Separovic, Andrew L Gundlach, Mohammed Akhter Hossain, John D Wade



Relaxin, a heterodimeric polypeptide hormone, is a key regulator of collagen metabolism and multiple vascular control pathways in humans and rodents. Its actions are mediated via its cognate G-protein-coupled receptor, RXFP1 although it also "pharmacologically" activates RXFP2, the receptor for the related, insulin-like peptide 3 (INSL3), which has specific actions on reproduction and bone metabolism. Therefore, experimental tools to facilitate insights into the distinct biological actions of relaxin and INSL3 are required, particularly for studies of tissues containing both RXFP1 and RXFP2. Here, we chemically functionalized human (H2) relaxin, the RXFP1-selective relaxin analog H2:A(4-24)(..

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Awarded by NHMRC (Australia)

Funding Acknowledgements

This research was partially funded by NHMRC (Australia) Project Grants 508995 and 1023078 to John D. Wade, Mohammed Akhter Hossain, and Ross A. D. Bathgate and 1024885 to Andrew L. Gundlach. We are grateful to Sharon Layfield for assistance with biochemical assays. Linda J. Chan was the recipient of the David Hay Postgraduate Writing Up Award from The University of Melbourne. Mohammed Akhter Hossain was the recipient of a Florey Foundation Fellowship and Ross A. D. Bathgate, Andrew L. Gundlach, and John D. Wade are NHMRC (Australia) Research Fellows. Research at The Florey Institute of Neuroscience and Mental Health is supported by the Victorian Government Operational Infrastructure Support Program.