Characterization of Interactions between Heparin/Glycosaminoglycan and Adeno-associated Virus
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Authors
Zhang, F.
Beaudet, J.M.
Aguilera, Javier
Xie, Q.
Lerch, T.F.
Davulcu, O.
Colón, W.
Chapman, M.S.
Linhardt, Robert J.
Issue Date
2013-09-10
Type
Article
Language
ENG
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Alternative Title
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.
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.
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.
Publisher
American Chemical Society (ACS)
Terms of Use
Journal
Volume
Issue
PubMed ID
DOI
ISSN
15204995
62960
62960