Inhibition of thermolysin and Bacillus brevis neutral proteinase (NP) reactions with N‐(3‐(2′‐furyl)acryloyl)glycyl‐L‐leucinamide by organic solvents and some other simple organic compounds (alkanols, aromatic compounds etc., in total 33 substances) was studied. The enzymes showed very similar affinities for the inhibitors in the whole range of Ki variation (3.7 orders of magnitude). A linear dependence with a nearly unitary slope between the pKi values and log P's of the compounds was found. The inhibitory power of the compounds, whose molecules are longer than those of propanol or benzene, depended on their ability to donate a hydrogen bond. pKi's of the compounds, in which substituents attached to the propyl group or benzene ring are unable to donate the hydrogen bond, fell off the correlation line; the deviation was proportional to the van der Waals volume of the substituent. pKi's of tert‐butanol and cyclohexanol also fell off the correlation line. Geometrical thickness of their molecules exceeds that of the other studied inhibitors; this may explain their lowered affinity for the enzymes. 6,6‐ or 7,5‐bicyclic compounds did not inhibit these enzymes.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.