A chondroitin sulfate purified from shark cartilage and bovine serum albumin interaction activity
Copyright © 2024. Published by Elsevier B.V..
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.
Medienart: |
E-Artikel |
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Erscheinungsjahr: |
2024 |
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Erschienen: |
2024 |
Enthalten in: |
Zur Gesamtaufnahme - volume:260 |
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Enthalten in: |
International journal of biological macromolecules - 260(2024), Pt 1 vom: 19. Feb., Seite 129499 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Pang, Hai-Long [VerfasserIn] |
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Links: |
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Themen: |
27432CM55Q |
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Anmerkungen: |
Date Completed 28.02.2024 Date Revised 28.02.2024 published: Print-Electronic Citation Status MEDLINE |
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doi: |
10.1016/j.ijbiomac.2024.129499 |
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funding: |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM367532530 |
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520 | |a Copyright © 2024. Published by Elsevier B.V. | ||
520 | |a 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 | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Bovine serum albumin | |
650 | 4 | |a Chondroitin sulfate | |
650 | 4 | |a Fluorescence quenching | |
650 | 4 | |a Molecular docking | |
650 | 7 | |a Serum Albumin, Bovine |2 NLM | |
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650 | 7 | |a Chondroitin Sulfates |2 NLM | |
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700 | 1 | |a Liu, Peng |e verfasserin |4 aut | |
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700 | 1 | |a Zhang, Li-Tao |e verfasserin |4 aut | |
700 | 1 | |a Ren, Qiang |e verfasserin |4 aut | |
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