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Updated: Mar 6, 2026
Colorimetric Analysis of Alkaline Phosphatase Activity in S. aureus Biofilm
Published on: April 12, 2019
Coumarin sulfonates: New alkaline phosphatase inhibitors; in vitro and in silico studies
Uzma Salar1, Khalid Mohammed Khan1, Jamshed Iqbal2
1H. E. J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan.
Abstract:
A library of coumarin derived sulfonyl esters (1-38) was synthesized by reacting various hydroxy coumarins with different alkyl and aryl sulfonyl chlorides. All compounds were evaluated for their potential to inhibit alkaline phosphatases (hTNAP and hIAP). Most of the compounds were found to be inhibitors of APs. Compound 20 was found to be the most active hIAP inhibitor (IC50 = 1.11 ± 0.15 μM), whereas, compound 13 was found to be the most active hTNAP inhibitor (IC50 = 0.58 ± 0.17 μM). Detailed structure activity relationship studies (SAR), and molecular docking studies were carried out to identify structural elements necessary for AP inhibition, in addition to rationalize most probable binding site interaction of the inhibitors with the AP enzymes.
