Menon, Vishnu and Rao, Mala (2012) A low molecular weight aspartic protease inhibitor from a novel Penicillium sp: Implications in combating fungal infections. Microbiology, 158. pp. 1897-1907.

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The article reports for the first time the isolation and characterization of a low molecular weight aspartic protease inhibitor from a novel Penicillium sp. The inhibitor was purified to homogeneity as shown by rp-HPLC and SDS-PAGE. The Mr of the inhibitor was 1585 and the amino acid composition showed the presence of D, D, D, E, A, K, L, Y, H, I, W residues. The steady-state kinetic interactions of Aspergillus saitoi aspartic protease with the inhibitor exhibited reversible, competitive, time-dependent tight binding nature of the inhibitor with IC50 and Ki values of 1.8 µM and 0.85 µM respectively. The fluorescence and CD analysis deciphered the inactivation of the enzyme due to binding of the inhibitor to the active site. The inhibitor was found to inhibit mycelial growth and spore germination of A. fumigatus and A. niger in vitro with MIC values of 1.65 and 0.30 μg/ml respectively. The finding of the inhibitor will potentially open the way towards the development of tight binding peptidic inhibitor against fungal aspartic protease to combat human fungal infections.

Item Type: Article
Subjects: Biological Sciences
Depositing User: Mr Vishnu Menon
Date Deposited: 05 Feb 2013 11:17
Last Modified: 05 Feb 2013 11:17

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