A chondroitin sulfate purified from shark cartilage and bovine serum albumin interaction activity.

Autor: Pang HL; Department of Pharmacy, Weifang Medical University, Weifang, Shandong, China; Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China., Lu H; Department of Pharmacy, Weifang Medical University, Weifang, Shandong, China; Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China., Liu P; Rizhao Science and Technology Innovation Service Center, Rizhao, Shandong, China., Zhang YT; Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China. Electronic address: zhangyt@mail.jnmc.edu.cn., Zhang LT; Department of Biological Science, Jining Medical University, Rizhao, Shandong, China. Electronic address: zhanglitao@mail.jnmc.edu.cn., Ren Q; Department of Pharmacy, Jining Medical University, Rizhao, Shandong, China. Electronic address: renqiang@mail.jnmc.edu.cn.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Mar; Vol. 260 (Pt 1), pp. 129499. Date of Electronic Publication: 2024 Jan 22.
DOI: 10.1016/j.ijbiomac.2024.129499
Abstrakt: Chondroitin sulfate (CS) was extracted and purified from shark cartilage, and its interaction with bovine serum albumin (BSA) were studied. The content of chondroitin sulfate in shark cartilage was 29.97 % using the 1,9-dimethyl-methylene blue method. The molecular weight of CS was determined to be 62.464 kDa by high-performance gel permeation chromatography. UV and FT-IR spectroscopy identified the characteristics of CS and its functional group information. NMR spectroscopy and disaccharide derivatization revealed that CS was predominantly composed of disulfated disaccharides, specifically ΔDi4,6S. Fluorescence quenching experiments indicated that the interaction between CS and BSA exhibited static quenching, with a binding site number of 1. The binding process was primarily mediated by van der Waals forces and hydrogen bonds. Furthermore, synchronous and 3D fluorescence spectroscopy demonstrated that CS had minimal impact on the polarity and hydrophobicity of the microenvironment surrounding Tyr and Trp residues. UV-vis absorption and circular dichroism (CD) spectroscopy demonstrated the altered structure of BSA. The molecular docking analysis revealed that CS formed hydrogen bonds and salt bridges with BSA, predominantly binding to the IIA substructure domain of BSA. Investigating the interaction between CS and BSA holds the potential for enhancing its applications in drug delivery and tissue engineering endeavors.
Competing Interests: Declaration of competing interest The materials discussed herein have not been published elsewhere before, and the manuscript has not been submitted to any other journals.
(Copyright © 2024. Published by Elsevier B.V.)
Databáze: MEDLINE
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