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Multispectroscopic Exploration and Molecular Docking Analysis on Interaction of Eriocitrin With Bovine Serum Albumin

Multispectroscopic Exploration and Molecular Docking Analysis on Interaction of Eriocitrin With Bovine Serum Albumin

Xiangyu Cao, Zhijun Yang, Yonglin He, Ying Xia, Yin He, Jianli Liu

J Mol Recognit. 2019 Jul;32(7):e2779.

PMID: 30701606

Abstract:

Eriocitrin is a flavanone glycoside, which exists in lemon or lime citrus fruits. It possesses antioxidant, anticancer, and anti-allergy activities. In order to investigate the pharmacokinetics and pharmacological mechanisms of eriocitrin in vivo, the interaction between eriocitrin and bovine serum albumin (BSA) was studied under the simulated physiological conditions by multispectroscopic and molecular docking methods. The results well indicated that eriocitrin and BSA formed a new eriocitrin-BSA complex because of intermolecular interactions, which was demonstrated by the results of ultraviolet-visible (UV-vis) absorption spectra. The intrinsic fluorescence of BSA was quenched by eriocitrin, and static quenching was the quenching mechanism. The number of binding sites (n) and binding constant (Kb ) at 310 K were 1.22 and 2.84 × 106 L mol-1 , respectively. The values of thermodynamic parameters revealed that the binding process was spontaneous, and the main forces were the hydrophobic interaction. The binding distance between eriocitrin and BSA was 3.43 nm. In addition, eriocitrin changed the conformation of BSA, which was proved by synchronous fluorescence and circular dichroism (CD) spectra. The results of site marker competitive experiments suggested that eriocitrin was more likely to be inserted into the subdomain IIA (site I), which was further certified by molecular docking studies.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP13463280	Eriocitrin		13463-28-0	Price

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