De novo design and synthesis of cyclic and linear peptides to mimic the binding cassette of human relaxin.
A synthetic cyclic regioselectively addressable functionalized template was used to prepare six analogs that presented the side chains of the key receptor-binding residues of each of H2 and H3 relaxins and insulin-like peptide 3. None showed any binding affinity for RXFP1, RXFP2, or RXFP3, indicating that the key residues were either incorrectly oriented or that additional residues are required for receptor binding.
Howard Florey Institute, University of Melbourne, Parkville, Victoria, Australia.
Mohammed Akhter
MA
Hossain
Ross A D
RA
Bathgate
Geoffery
G
Tregear
John D
JD
Wade
D006801:Humans; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D043562:Receptors, G-Protein-Coupled / Q000737:chemistry / Q000378:metabolism; D018000:Receptors, Peptide / Q000737:chemistry / Q000378:metabolism; D012065:Relaxin / Q000031:analogs & derivatives / Q000138:chemical synthesis* / Q000737:chemistry* / Q000378:metabolism
D010455:Peptides; C417543:RXFP1 protein, human; D043562:Receptors, G-Protein-Coupled; D018000:Receptors, Peptide; D012065:Relaxin