Fibrinopeptide A binds Gly-Pro-Arg-Pro.
The tetrapeptide Gly-Pro-Arg-Pro inhibits fibrinogen aggregation, probably by binding to the same sites used during initiation of fibrin formation. The Gly-Pro-Arg-Pro binding sites have not yet been identified. However, their possible sequence and locations have been predicted on the basis of the amino acid pairing hypothesis. One of these predicted sites is on fibrinopeptide A. We report here that nuclear magnetic resonance studies indicate that Gly-Pro-Arg-Pro binds to fibrinopeptide A with a binding constant, K, of ca. 10(4) per mol. We also report results of 19 related peptide combinations used as controls.
D000595:Amino Acid Sequence; D001665:Binding Sites; D003701:Delta Sleep-Inducing Peptide; D005340:Fibrinogen / Q000378:metabolism*; D005344:Fibrinopeptide A / Q000378:metabolism*; D005345:Fibrinopeptide B / Q000378:metabolism; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides / Q000378:metabolism*
D009842:Oligopeptides; D005344:Fibrinopeptide A; D005345:Fibrinopeptide B; C034585:glycyl-prolyl-arginyl-proline; D003701:Delta Sleep-Inducing Peptide; D005340:Fibrinogen