American Chemical Society
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Inhibition of a Protein Tyrosine Phosphatase Using Mesoporous Oxides

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journal contribution
posted on 2010-03-11, 00:00 authored by S. Kapoor, T. S. Girish, S. S. Mandal, B. Gopal, A. J. Bhattacharyya
The feasibility of utilizing mesoporous matrices of alumina and silica for the inhibition of enzymatic activity is presented here. These studies were performed on a protein tyrosine phosphatase by the name chick retinal tyrosine phosphotase-2 (CRYP-2), a protein that is identical in sequence to the human glomerular epithelial protein-1 and involved in hepatic carcinoma. The inhibition of CRYP-2 is of tremendous therapeutic importance. Inhibition of catalytic activity was examined using the sustained delivery of p-nitrocatechol sulfate (pNCS) from bare and amine functionalized mesoporous silica (MCM-48) and mesoporous alumina (Al2O3). Among the various mesoporous matrices employed, amine functionalized MCM-48 exhibited the best release of pNCS and also inhibition of CRYP-2. The maximum speed of reaction vmax (=160 ± 10 μmol/mnt/mg) and inhibition constant Ki (=85.0 ± 5.0 μmol) estimated using a competitive inhibition model were found to be very similar to inhibition activities of protein tyrosine phosphatases using other methods.