Journal article
Design, synthesis, and characterization of a single-chain peptide antagonist for the relaxin-3 receptor RXFP3
LM Haugaard-Kedström, F Shabanpoor, MA Hossain, RJ Clark, PJ Ryan, DJ Craik, AL Gundlach, JD Wade, RAD Bathgate, KJ Rosengren
Journal of the American Chemical Society | AMER CHEMICAL SOC | Published : 2011
DOI: 10.1021/ja110567j
Abstract
Relaxin-3 is a two-chain disulfide-rich peptide that is the ancestral member of the relaxin peptide family and, together with its G protein-coupled receptor RXFP3, is highly expressed in the brain. Strong evolutionary conservation of relaxin-3 suggests a critical biological function and recent studies have demonstrated modulation of sensory, neuroendocrine, metabolic, and cognitive systems. However, detailed studies of central relaxin-3-RXFP3 signaling have until now been severely hampered by the lack of a readily available high-affinity antagonist for RXFP3. Previous studies have utilized a complex two-chain chimeric relaxin peptide, R3(BΔ23-27)R/I5, in which a truncated relaxin-3 B-chain c..
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Funding Acknowledgements
This work was supported by grants from the foundations Bengt Lundquist Minne and Helge Ax:son-Jonson Stiftelse to L.M.H.-K and the Faculty of Natural Science and Engineering, Linnaeus University, to K.J.R. Work in the laboratories of A.L.G., D.J.C., J.D.W., and RA.D.B. was supported by the National Medical and Health Research Council (NHMRC) of Australia. K.J.R and R.J.C. are NHMRC Biomedical CDA Fellows. A.L.G. and R.A.D.B. are NHMRC Senior Research Fellows. D.J.C and J.D.W. are NHMRC Principal Research Fellows. R.J.C. gratefully acknowledges the Australian Academy of Science for travel funding. We thank Sharon Layfield for providing transfected cells for the binding and signaling assays.