690674-36-3Relevant academic research and scientific papers
A Silanediol Inhibitor of the Metalloprotease Thermolysin: Synthesis and Comparison with a Phosphinic Acid Inhibitor
Kim, Jaeseung,Sieburth, Scott McN.
, p. 3008 - 3014 (2007/10/03)
A silanediol inhibitor of the metalloprotease thermolysin was prepared for comparison to a known phosphinic acid inhibitor, providing the first comparison of these second-row element based transition-state analogues. Inhibition of thermolysin by the silanediol (Ki = 41 nM) was comparable to that of the phosphinic acid (Ki = 10 nM) even though the silanediol is uncharged and thereby lacks the intrinsic Coulombic attraction of the phosphinate anion to the active-site zinc cation. This silanediol protease inhibitor is the least sterically encumbered example prepared to date and, therefore, the most prone toward polymerization. Hydrolysis of a difluorosilane intermediate to the silanediol leads cleanly to a monomeric product.
