Characterization of Neuwiedin, a new disintegrin from Bothrops neuwiedi venom gland with distinct cysteine pattern.

摘要: Disintegrins are cysteine-rich toxins containing the RGD motif exposed in a loop that binds integrins such as αIIbβ3, α5β1 and αvβ3. The flexibility of loop, controlled by profile cysteine pairs residues flanking sequence, key structural features for functional activity these molecules. Recently, our group reported transcript venom gland Bothrops neuwiedi corresponding to new P-II SVMP precursor, BnMPIIx, which RGD-binding includes many substituted unique at C-terminal. In this paper, we obtained recombinant disintegrin domain Neuwiedin, inhibited ADP-induced platelet aggregation, endothelial cell adhesion fibrinogen tube formation Matrigel with no particular selectivity αIIbβ3 or integrins. This value was also comparable inhibition observed other disintegrins conserved positions loop. regard, Neuwiedin is an important component understand relevance diversity generated accelerated evolution well find out eventual disintegrin-dependent targets may be approached disintegrins.