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- W2086766155 abstract "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 beta-phenylethyl group at the P1' position, suggesting a small hydrophobic channel into the S1' subsite of stromelysin. One particular compound, N-[1(R)-carboxyethyl]-alpha(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." @default.
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- W2086766155 date "1993-12-01" @default.
- W2086766155 modified "2023-09-27" @default.
- W2086766155 title "Inhibition of matrix metalloproteinases by N-carboxyalkyl peptides" @default.
- W2086766155 doi "https://doi.org/10.1021/jm00078a019" @default.
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