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Abstract
Abstract
Human (h) carbonic anhydrase (CAs, EC 4.2.1.1) isoforms IX and XII were recently confirmed as anticancer targets against solid hypoxic tumours. The “three-tails approach” has been proposed as an extension of the forerunner “tail” and “dual-tail approach” to fully exploit the amino acid differences at the medium/outer active site rims among different hCAs and to obtain more isoform-selective inhibitors. Many three-tailed inhibitors (TTIs) showed higher selectivity against the tumour-associated isoforms hCA IX and XII with respect to the off-targets hCA I and II. X-ray crystallography studies were performed to investigate the binding mode of four TTIs in complex with a hCA IX mimic. The ability of the most potent and selective TTIs to reduce
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1 Department NEUROFARBA – Pharmaceutical and Nutraceutical Section, University of Firenze , Florence , Italy, Department NEUROFARBA – Pharmaceutical and Nutraceutical Section, Laboratory of Molecular Modeling Cheminformatics & QSAR, University of Firenze , Florence , Italy
2 Department NEUROFARBA – Pharmaceutical and Nutraceutical Section, University of Firenze , Florence , Italy
3 Department of Biochemistry and Molecular Biology, College of Medicine, University of Florida , Gainesville , FL , USA
4 Chemistry Department, College of Science, King Saud University , Riyadh , Saudi Arabia
5 Department NEUROFARBA – Pharmaceutical and Nutraceutical Section, Laboratory of Molecular Modeling Cheminformatics & QSAR, University of Firenze , Florence , Italy