Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
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Probing the Interaction of Dengue Virus Envelope Protein with Heparin: Assessment of Glycosaminoglycan-Derived Inhibitors, R.M. Marks, H. Lu, R. Sundaresan, T. Toida, A. Suzuki, T. Imanari, M.J. Hernaiz, R. J. Linhardt, Journal of Medicinal Chemistry, 44, 2178-2187, 2001.
A structure-activity relationship study was carried out to facilitate development of inhibitors of dengue virus infectivity. Previous studies demonstrated that a highly charged heparan sulfate, a heparin-like glycosaminoglycan found on the cell surface, serves as a receptor for dengue virus by binding to its envelope protein. Interventions that disrupt this binding effectively inhibit infectivity. A competitive binding assay was developed to screen polyanionic compounds for activity in preventing binding of dengue virus envelope protein to immobilized heparin; compounds tested included drugs, excipients, and larger glycosaminoglycans and their semisynthetic derivatives. Results of this competitive binding assay were used to select agents for detailed evaluation of interactions by surface plasmon resonance spectroscopy, which afforded binding on-rates, off-rates, and dissociation constants. From these data, an understanding of the structural requirements for polyanion binding to dengue virus envelope protein has been established.;
Journal of Medicinal Chemistry, 44, 2178-2187; 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.
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Journal of Medicinal Chemistry; https://harc.rpi.edu/;