Structural determinants of the selectivity of KTS-disintegrins for the α1β1 integrin

摘要: KTS-disintegrins are a subfamily of short monomeric disintegrins that potent and selective inhibitors α1β1 integrin. The amino acid sequence the new KTS-disintegrin, viperistatin, differs from previously characterized obtustatin in three residues at position 24 (within integrin binding loop), 38 (hydrophobic core) 40 (C-terminal region). Noteworthy, viperistatin is about 25-fold more than inhibiting this to collagen IV. Synthetic peptides representing full-length integrin-binding loops these showed Leu24/Arg substitution appears be partly responsible for increased inhibitory activity over obtustatin.