154096-58-9Relevant articles and documents
Inhibition of matrix metalloproteinases by N-carboxyalkyl peptides
Chapman,Kopka,Durette,Esser,Lanza,Izquierdo- Martin,Niedzwiecki,Chang,Harrison,Kuo,Lin,Stein,Hagmann
, p. 4293 - 4301 (2007/10/02)
An extensive study of the requirements for effective binding of N- carboxyalkyl peptides to human stromelysin, collagenase, and to a lesser extent, gelatinase A has been investigated. These efforts afforded inhibitors generally in the 100-400 nM range for these matrix metalloproteinases. The most significant increase in potency was obtained with the introduction of a β-phenylethyl group at the P1' position, suggesting a small hydrophobic channel into the S1' subsite of stromelysin. One particular compound, N- [1(R)-carboxyethyl]-α(S)-(2-phenylethyl)glycyl-L-leucine, N-phenylamide (79a), is relatively selective for rabbit stromelysin with a K(i) = 6.5 nM and may prove useful for elucidating the role of endogenously-produced stromelysin in lapine models of tissue degradation.