Molecular Docking and Reaction Kinetic Studies of Chrysin Binding to Serum Albumin

Jiang, Bingli; Zhao, Anran; Jin, Miao; Chang, Pengfei; Chen, Hailin; Pan, Weiyi; Lin, Cui-Wu

doi:10.1177/1934578x1400900215

Cited by 1 publication

(1 citation statement)

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“…Chrysin and baicalein have higher affinities for BSA and HSA than flavone, but lower than the affinities of 7-HA [65]. Computational models have suggested that chrysin binds to the IB subdomain of the albumin [66], whereas experimental data indicate that baicalein [67], wogonin [68,69], and 3,7-dihydroxyflavone [70] bind to the IIA subdomain (site I of HSA and BSA).…”

Section: Albumin Bindingmentioning

confidence: 99%

Pharmacokinetics of B-Ring Unsubstituted Flavones

et al. 2019

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B-ring unsubstituted flavones (of which the most widely known are chrysin, baicalein, wogonin, and oroxylin A) are 2-phenylchromen-4-one molecules of which the B-ring is devoid of any hydroxy, methoxy, or other substituent. They may be found naturally in a number of herbal products used for therapeutic purposes, and several have been designed by researchers and obtained in the laboratory. They have generated interest in the scientific community for their potential use in a variety of pathologies, and understanding their pharmacokinetics is important for a grasp of their optimal use. Based on a comprehensive survey of the relevant literature, this paper examines their absorption (with deglycosylation as a preliminary step) and their fate in the body, from metabolism to excretion. Differences among species (inter-individual) and within the same species (intra-individual) variability have been examined based on the available data, and finally, knowledge gaps and directions of future research are discussed.

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