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    Cytochrome P450 (inhibitors for the metabolism of drugs)
    (Elsevier, 2023) Akdemir, A.
    Drug-metabolizing enzymes, such as P450 3A4, are key determinants of the pharmacokinetics of drugs and as such are key factors in pharmacotherapy. Pharmacokinetic enhancers, also known as pharmacokinetic boosters, cause intended drug-drug interactions by inhibiting drug-metabolizing enzymes and increasing the bioavailability of target drugs. In this chapter, the focus will be mainly on the structure, function and physiology of the most important drug metabolizing P450 enzyme 3A4 as well as its inhibitors with a specific emphasis on pharmacokinetic boosters. © 2024 Elsevier Inc. All rights reserved.
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    Thiosemicarbazone-benzenesulfonamide Derivatives as Human Carbonic Anhydrases Inhibitors: Synthesis, Characterization, and In silico Studies
    (Bentham Science Publishers, 2024) Trawally, M.; Demir-Yazıcı, K.; Angeli, A.; Kaya, K.; Akdemir, A.; Supuran, C.T.; Güzel-Akdemir Ö.
    Introduction: Carbonic anhydrases (CAs) are widespread metalloenzymes with the core function of catalyzing the interconversion of CO2 and HCO3-. Targeting these enzymes using selective inhibitors has emerged as a promising approach for the development of novel therapeutic agents against multiple diseases. Methods: A series of novel thiosemicarbazone-containing derivatives were synthesized, characterized, and tested for their inhibitory activity against pharmaceutically important human CA I (hCA I), II (hCA II), IX (hCA IX), and XII (hCA XII) using the single tail approach. Results: The compounds generally inhibited the isoenzymes at low nanomolar concentrations, with compound 6b having Ki values of 7.16, 0.31, 92.5, and 375 nM against hCA I, II, IX and XII, respectively. Compound 6e exhibited Ki values of 27.6, 0.34, 872, and 94.5 nM against hCA I, II, IX and XII, respectively. Conclusion: To rationalize the inhibition data, molecular docking studies were conducted, providing insight into the binding mechanisms, molecular interactions, and selectivity of the compounds towards the isoenzymes. © 2024 Bentham Science Publishers.