Interactions of Three Chalcones with Human Serum Albumin Revealed by Spectroscopic Techniques

Ma, Ji; Fan, Yun-Chang; Si, Qingerile; Liu, Yuan; Wang, Xiangfeng; Liu, Hailing; Xie, Mengxia

doi:10.2116/analsci.33.493

Cited by 6 publications

(1 citation statement)

References 25 publications

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“…The UV absorption spectra of chalcones usually have one or two main bands. Band I (320-400 nm) is possible from the conjugated system of B-ring and the carbonyl group in the molecule and Band II (220-270 nm) is attributed to the absorption for the conjugated system of A-ring and the carbonyl group [39] .…”

Section: Resultsmentioning

confidence: 99%

Study on the interaction of some (E)-2-benzylidenebenzosuberone derivatives with serum albumin by UV-Vis method, inhibitory effect on topoisomerase

Rozmer

Perjési

2020

J Pharm Biopharm Res

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Interaction of some cyclic chalcone analogs, (E)-2-(4-X-benzylidene)-1-benzosuberone derivatives with bovine serum albumin (BSA) and human serum albumin (HSA) has been investigated using UV-Vis spectroscopic methods. Recording the UV-Vis spectra of compounds in the presence of BSA or HSA indicated interaction of the molecules with the hydrophobic binding site(s) of the proteins. Investigated analogs have shown remarkable topo I and topo II inhibitory activity compared to camptothecin and etoposide, respectively, at 40 µM concentration. The observed interactions between the cyclic chalcone analogs and the cellular macromolecules might play a role in the previously detected cytotoxicity against several tumor cell lines.

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Section: Resultsmentioning

confidence: 99%