Emina Mrkalić, Marina Ćendić Serafinović, Ratomir M. Jelić, Stefana Stojanović, Miroslav Sovrlić
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引用次数: 0
Abstract
Serum albumin is the major soluble protein in the circulatory system of humans. The metabolism of drugs, their distribution, free concentration, and efficacy depend on the drug-serum albumin interaction [1]. Accordingly, it is important to study the interactions of drugs with serum albumin, which determines the pharmacology and pharmacodynamics of drugs. Quercetin (QUE), a natural polyphenol widely distributed in many plant foods, such as fruits, vegetables, nuts, seeds, grains, and tea [2], bind to serum albumin [3]. Tigecycline (TGC), is a tetracycline antibiotic widely used in the treatment of bacterial infections [4]. This study aimed to investigate the binding properties of TGC to HSA in the presence of QUE, under physiological conditions, by fluorescence spectroscopy.
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