Author
Zhang, F.; Beaudet, J.M.; Aguilera, J.; Xie, Q.; Lerch, T.F.; Davulcu, O.; Colón, W.; Chapman, M.S.; Linhardt, Robert J.
Other Contributors
Date Issued
2013-09-10
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Characterization of Interactions between Heparin/Glycosaminoglycan and Adeno-associated Virus, F. Zhang, J.M. Beaudet, J. Aguilera, Q. Xie, T. F. Lerch, O. Davulcu, W. Colón, M. S. Chapman, R. J. Linhardt, Biochemistry, 52, 6275–6285, 2013.
Abstract
Adeno-associated virus (AAV) is a key candidate in the development of gene therapy. In this work, we used surface plasmon resonance spectroscopy to study the interaction between AAV and heparin and other glycosaminoglycans (GAGs). Surface plasmon resonance results revealed that heparin binds to AAV with an extremely high affinity. Solution competition studies showed that binding of AAV to heparin is chain length-dependent. AAV prefers to bind full chain heparin. All sulfo groups (especially N-sulfo and 6-O-sulfo groups) on heparin are important for the AAV-heparin interaction. Higher levels of sulfo group substitution in GAGs enhance their binding affinities. Atomic force microscopy was also performed to image AAV-2 in a complex with heparin.;
Description
Biochemistry, 52, 6275–6285; 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);
Publisher
American Chemical Society (ACS)
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Biochemistry; https://harc.rpi.edu/;
Access
A full text version is available in DSpace@RPI;
