Isolation and Amino Acid Sequence of Flavostatin, a Novel Disintegrin From the Venom of Trimeresurus flavoviridis

Abstract

Maruyama, K., T. Kawasaki, Y. Sakai, Y. Taniuchi, M. Shimizu, H. Kawashima and T. Takenaka. Isolation and amino acid sequence of flavostatin, a novel disintegrin from the venom of Trimeresurus flavoviridis. Peptides 18(1)73–78, 1997—Flavostatin, a novel disintegrin purified from the venom of Trimeresurus flavoviridis, consists of 68 amino acids, including an Arg-Gly-Asp sequence and 12 Cys residues at positions highly conserved among disintegrins. The N-terminal sequence of flavostatin was identical to those of triflavin and flavoridin, previously reported disintegrins from the Trimeresurus flavoviridis venom. Differences among the C-terminal sequences of these disintegrins are considered to affect their biological potencies. Isolated flavostatin inhibited ADP, collagen, and thrombin receptor agonist peptide-induced platelet aggregation in human platelet-rich plasma with an IC 50 range of 59 to 98 n M. Contrary to expectations, these values were similar to those for triflavin.