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Design, synthesis, ...
Design, synthesis, and characterization of a single-chain peptide antagonist for the relaxin-3 receptor RXFP3
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- Haugaard-Kedström, Linda M. (författare)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV
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- Shabanpoor, Fazel (författare)
- Florey Neuroscience, The University of Melbourne
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- Hossain, Mohammed Akhter (författare)
- Florey Neuroscience, The University of Melbourne
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- Clark, Richard (författare)
- The University of Queensland, Institute for Molecular Bioscience
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- Ryan, Philip (författare)
- Florey Neuroscience, The University of Melbourne
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- Craik, David (författare)
- The University of Queensland, Institute for Molecular Bioscience
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- Gundlach, Andrew (författare)
- Florey Neuroscience, The University of Melbourne
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- Wade, John (författare)
- Florey Neuroscience, The University of Melbourne
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- Bathgate, Ross (författare)
- Florey Neuroscience, The University of Melbourne
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- Rosengren, K. Johan (författare)
- Linnéuniversitetet,Institutionen för naturvetenskap, NV,BBCL
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(creator_code:org_t)
- 2011-03-08
- 2011
- Engelska.
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Ingår i: Journal of the American Chemical Society. - : American Chemical Society (ACS). - 0002-7863 .- 1520-5126. ; 133:13, s. 4965-4974
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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(B Delta 23-27)R/I5, in which a truncated relaxin-3 B-chain carrying an additional C-terminal Arg residue was combined with the insulin-like peptide S (INSL5) A-chain. In this study we demonstrate that, by replacing the native Cys in this truncated relaxin-3 B-chain with Ser, a single-chain linear peptide of 23 amino acids that retains high-affinity antagonism for RXFP3 can be achieved. In vivo studies demonstrate that this peptide, R3 B1-22R, antagonized relaxin-3/RXFP3 induced increases in feeding in rats after intracerebroventricular injection. Thus, R3 B1-22R represents an excellent tool for biological studies probing relaxin pharmacology and a lead molecule for the development of synthetically tractable, single-chain RXFP3 modulators for clinical use.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- Biokemi
- Biochemistry
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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