Characterization of resistance to a potent d-peptide HIV entry inhibitor
Characterization of resistance to a potent d-peptide HIV entry inhibitor
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Author / Creator
Smith, Amanda R. , Weinstock, Matthew T. , Siglin, Amanda E. , Whitby, Frank G. , Francis, J. Nicholas , Hill, Christopher P. , Eckert, Debra M. , Root, Michael J. , Kay, Michael S. and SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
Publisher
England: BioMed Central Ltd
Journal title
Language
English
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Publisher
England: BioMed Central Ltd
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Scope and Contents
Contents
PIE12-trimer is a highly potent D-peptide HIV-1 entry inhibitor that broadly targets group M isolates. It specifically binds the three identical conserved hydrophobic pockets at the base of the gp41 N-trimer with sub-femtomolar affinity. This extremely high affinity for the transiently exposed gp41 trimer provides a reserve of binding energy (resis...
Alternative Titles
Full title
Characterization of resistance to a potent d-peptide HIV entry inhibitor
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Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_afdf95a93d6b45de92747e1a8e5821fd
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_afdf95a93d6b45de92747e1a8e5821fd
Other Identifiers
ISSN
1742-4690
E-ISSN
1742-4690
DOI
10.1186/s12977-019-0489-7
