Journal
ACS MEDICINAL CHEMISTRY LETTERS
Volume 9, Issue 8, Pages 797-802Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acsmedchemlett.7b00364
Keywords
Chemical probes; glycoprotein D; glycosaminoglycans; heparan sulfate mimetics; herpes simplex virus
Categories
Funding
- Midwestern University
- National Center for Research Resources [S10 RR027411]
- NIH [HL090586, HL107152, HL128639]
- NATIONAL CENTER FOR RESEARCH RESOURCES [S10RR027411] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL090586, R25HL128639, P01HL107152] Funding Source: NIH RePORTER
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Although heparan sulfate (HS) has been implicated in facilitating entry of enveloped viruses including herpes simplex virus (HSV), small molecules that effectively compete with this abundant, cell surface macromolecule remain unknown. We reasoned that entry of HSV-1 involving its glycoprotein D (gD) binding to HS could be competitively targeted through small, synthetic, nonsaccharide glycosaminoglycan mimetics (NSGMs). Screening a library of NSGMs identified a small, distinct group that bound gD with affinities of 8-120 nM. Studies on HSV-1 entry into HeLa, HFF-1, and VK2/E6E7 cells identified inhibitors with potencies in the range of 0.4-1.0 mu M. These synthetic NSGMs are likely to offer promising chemical biology probes and/or antiviral drug discovery opportunities.
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