Structural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage

Authors
Li, Q.
Li, G.
Zhao, X.
Shan, X.
Cai, C.
Zhao, J.
Zhang, F.
Linhardt, Robert J.
Yu, G.
ORCID
https://orcid.org/0000-0003-2219-5833
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Issue Date
2018
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
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Terms of Use
Attribution 3.0 United States
CC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
Full Citation
Structural characterization and interaction with RCA120 of a highly sulfated keratan sulfate from blue shark (Prionace glauca) cartilage, Q. Li, G. Li, X.Zhao, X. Shan, C. Cai, J. Zhao, F. Zhang, R. J. Linhardt, G. Yu, Marine Drugs, 16, 128, 2018.
Abstract
As an important glycosaminoglycan, keratan sulfate (KS) mainly exists in corneal and cartilage, possessing various biological activities. In this study, we purified KS from blue shark (Prionace glauca) cartilage and prepared KS oligosaccharides (KSO) through keratanase II-catalyzed hydrolysis. The structures of KS and KSO were characterized using multi-dimensional nuclear magnetic resonance (NMR) spectra and liquid chromatography-mass spectrometry (LC-MS). Shark cartilage KS was highly sulfated and modified with ~2.69% N-acetylneuraminic acid (NeuAc) through α(2,3)-linked to galactose. Additionally, KS exhibited binding affinity to Ricinus communis agglutinin I (RCA120) in a concentration-dependent manner, a highly toxic lectin from beans of the castor plant. Furthermore, KSO from dp2 to dp8 bound to RCA120 in the increasing trend while the binding affinity of dp8 was superior to polysaccharide. These results define novel structural features for KS from Prionace glauca cartilage and demonstrate the potential application on ricin-antidote exploitation.
Description
Marine Drugs, 16, 128
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Multidisciplinary Digital Publishing Institute (MDPI)
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI
CC BY — Creative Commons Attribution