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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Substrate analogue inhibitors of the IgA1 proteinases from Neisseria gonorrhoeae.

Substrate analogues based on the amino acid sequence of the hinge region of human IgA1 around the cleavage site of the IgA1 proteinases secreted by Neisseria gonorrhoeae are competitive inhibitors of these enzymes. The octapeptide Thr-Pro-Pro-Thr-Pro-Ser-Pro-Ser, which occurs between residues 233 and 240, has an IC50 value of 0.26 mM for the type 1 proteinase and 0.50 mM for the type 2 enzyme. Acetylation of the octapeptide N-terminal amino group lowers affinity for the type 1 proteinase sixfold but does not change binding to the type 2 enzyme. Amidation of the C-terminal carboxyl group does not change binding to the type 1 proteinase but improves IC50 for the type 2 enzyme. Simultaneous blockade of both the N- and C-termini drastically lowers affinity of the octapeptide for both proteinases. Sequential replacement of the hydroxy amino acids in the blocked octapeptide with cysteine yields a series of inhibitors that generally bind to the neisserial IgA1 proteinases as well as or better than the unblocked octapeptide. The most effective inhibitor contains a cysteine residue at position 6 (P3') and has an IC50 value for the type 2 IgA1 proteinase of 50 microM. Dimerization of the cysteine-containing octapeptides significantly diminishes inhibitory properties. The substrate analogues described here are the first synthetic inhibitors of the neisserial IgA1 proteinases to be reported.[1]


  1. Substrate analogue inhibitors of the IgA1 proteinases from Neisseria gonorrhoeae. Burton, J., Wood, S.G., Lynch, M., Plaut, A.G. J. Med. Chem. (1988) [Pubmed]
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