Characterization of two platelet aggregation inhibitor-like polypeptides from viper venom (original) (raw)

The study presents the characterization of two platelet aggregation inhibitor-like polypeptides, eristocophins I and II, derived from leaf-nosed viper venom. These polypeptides are analyzed for their structures, particularly their RGD and WND motifs, which are integral to their biologically active roles in inhibiting platelet aggregation. Findings suggest significant amino acid conservation and potential interactions with various platelet-adhesive glycoproteins, emphasizing their therapeutic relevance.