Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8334664 | International Journal of Biological Macromolecules | 2012 | 10 Pages |
Abstract
The present article reports a low molecular weight aspartic protease inhibitor from a Streptomyces sp. MBR04 exhibiting a two-step inhibition mechanism against pepsin. The kinetic interactions revealed a reversible, competitive, slow-tight binding inhibition with an IC50 and Ki values of 4.5Â nM and 4Â nM respectively. The conformational changes induced upon inhibitor binding to pepsin was monitored by far and near UV analysis, demonstrated that the inhibitor binds to the active site and causes inactivation. Chemical modification of the inhibitor with WRK and TNBS abolished the antiproteolytic activity of the inhibitor.
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Authors
Vishnu Menon, Mala Rao,