Enzymatic Synthesis of Heparin Related Polysaccharides on Sensor Chips: Rapid Screening of Heparin-Protein Interactions
Authors
Muñoz, Eva
Xu, Ding
Avci, Fikri
Kemp, Melissa
Liu, Jian
Linhardt, Robert J.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2006-01-13
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
Terms of Use
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Full Citation
Enzymatic Synthesis of Heparin Related Polysaccharides on Sensor Chips: Rapid Screening of Heparin-Protein Interactions, E. Muñoz, D. Xu, F. Avci, M. Kemp, J. Liu, R. J. Linhardt, Biochemical and Biophysical Research Communications , 339, 597-602, 2006.
Abstract
The biological roles of heparin (HP) and heparan sulfate (HS) are mediated mainly through their interaction with proteins. In the present work, we provide a rapid method for screening HP/HS–protein interactions providing structural data on the key sulfo groups that participate in the binding. A library of polysaccharides structurally related to HP was prepared by immobilizing the biotinylated N-sulfated K5 polysaccharide (N-sulfoheparosan) on sensor chips followed by selective modification of this polysaccharide with enzymes that participate in HP/HS biosynthesis. The polysaccharides synthesized on the surface of the sensor chips differ in the number and position of sulfo groups present both on uronic acid and glucosamine residues. Surface plasmon resonance was used to measure the interaction of each member of this polysaccharide library with antithrombin III (ATIII), to afford structural information on sulfo groups required for this HP/HS–protein interaction. This method is viewed as widely applicable for the study of the structure–activity relationship (SAR) of HP/HS–protein interactions.
Description
Biochemical and Biophysical Research Communications, 339, 597-602
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Elsevier
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
Biochemical and Biophysical Research Communications
https://harc.rpi.edu/
Rensselaer Polytechnic Institute, Troy, NY
Biochemical and Biophysical Research Communications
https://harc.rpi.edu/
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A full text version is available in DSpace@RPI