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標題: Highly potent and selective 4,4 '-biphenyl-4-acylate-4 '-N-n-butylcarbamate inhibitors of Pseudomonas species lipase
作者: Lin, G.
Chen, G.H.
Lu, Y.F.
Su, L.H.
Liao, P.S.
關鍵字: Pseudomonas species lipase
carbamate inhibitors
structure-reactivity relationships
cross-interaction correlations
pancreatic cholesterol esterase
steady-state kinetics
acetylcholinesterase inhibition
molecular recognition
binding site
期刊/報告no:: European Journal of Lipid Science and Technology, Volume 107, Issue 2, Page(s) 65-73.
摘要: 4,4'-Biphenyl-4-acylate-4'-N-n-butylcarbamates (1-8) are synthesized and characterized as highly potent and selective pseudo-substrate inhibitors of Pseudomonas species lipase. Thus, the n-butylcarbamate moieties of the inhibitors bind to the first acyl chain binding site (ACS) of the enzyme. Therefore, the ester moieties of the inhibitors may bind to the second ACS of the enzyme, due to the linear 4,4'-biphenyl moiety of the inhibitors. -logK(i), logk(2), and logk(i) values of carbamates 1-8 are multiply linearly correlated with the Taft steric constant (E-s) and the Hansch hydrophobicity constant (pi), but not with the Taft substituent constant (sigma*). For -logK(i), logk(2), and logk(i) correlations, values of delta are 0.8, 0.34, and 1.0, respectively, and values of psi are 1.0, 0.4, and 1.3, respectively. Positive delta and psi values for these correlations indicate that the second ACS of the enzyme prefers to bind to small and hydrophobic ester groups of the inhibitors. Among carbamates 1-8, carbamate 3, with a K-i value of 2.5 nM, is the most potent inhibitor.
ISSN: 1438-7697
Appears in Collections:期刊論文



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