AI Article Synopsis
- Researchers designed and synthesized stapled peptides with a biphenyl cross-linker to improve upon a previous HIV capsid assembly inhibitor.
- These biphenyl-stapled peptides showed significantly better cell penetration and antiviral effects compared to linear peptides in lab tests.
- The most effective stapled peptide binds to key HIV proteins, inhibiting both the virus's entry into cells and its assembly.
Article Abstract
Here we report the design and synthesis of a panel of stapled peptides containing a distance-matching biphenyl cross-linker based upon a peptide capsid assembly inhibitor reported previously. Compared with the linear peptide, the biphenyl-stapled peptides exhibited significantly enhanced cell penetration and potent antiviral activity in the cell-based infection assays. Isothermal titration calorimetry and surface plasmon resonance experiments revealed that the most active stapled CAI peptide binds to the C-terminal domain of HIV capsid protein as well as envelop glycoprotein gp120 with low micromolar binding affinities, and as a result, inhibits both the HIV-1 virus entry and the virus assembly.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4005879 | PMC |
| http://dx.doi.org/10.1016/j.bmcl.2014.02.038 | DOI Listing |
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