Inhibition Studies onVibrio choleraeNeuraminidase

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Abstract
A series of viral neuraminidase inhibitors showing no structural analogy to neuraminic acids were tested to find whether they are effective inhibitors of V. cholerae neuraminidase, too. The results obtained with the N-phenyloxamic acid derivatives [N-(4-nitrophenyl)oxamic acid (2), N-(4-nitrophenyl)oxamic acid ethyl ester (4), N-(4-hydroxyphenyl)oxamic acid ethyl ester (6), N-(4-hydroxyphenyl)oxamic acid (3) and N-(4-aminophenyl)oxamic acid ethyl ester (5)] and with simple aromatic compounds structurally related to R, i.e., 4-nitroaniline (7), N-acetyl-4-nitroaniline (8), 4-nitrophenol (9), 2,4-dinitrophenol (10) and 4-aminophenol (11) are reported. The inhibitory effects of 2-11 were studied in 0.1 M sodium acetate buffer, pH 5.5, 2 mM CaCl2, at 37.degree. C using the benzyl-.alpha.-ketoside of N-acetyl-D-neuraminic acid (1) as a substrate. The compounds 2-11 are competitive inhibitors of the enzymatic hydrolysis of the .alpha.-ketoside 1. The competitive inhibition kinetics are supported by the Lineweaver-Burke method. The inhibition constants (Ki) are in the range of 0.03-5.7 mM. The simple aromatic compounds 7-11 show higher inhibitory activities than the phenyloxamic acid derivatives 2-6. Significant differences in the Ki values were observed within the 2 series of inhibitors, whereby those containing a nitro group were most effective.

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