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• W2069401811 abstract "T-20/Fuzeon/Enfuvirtide (ENF), a peptide inhibitor of HIV-1 infection, targets the grooves created by heptad repeat 2 (HR2) of Env's coiled-coil, but mutants resistant to ENF emerge. In this study, ENF-resistant mutants--V38A, N43D, N43D/S138A, Q40H/L45M--were combined with modified inhibitory peptides to identify what we believe to be novel ways to improve peptide efficacy. V38A did not substantially reduce infectivity, but was relatively resistant to inhibitory peptides. N43D was more resistant to inhibitory peptides than wild-type, but infectivity was reduced. The additional mutation S138A (N43D/S138A) increased infectivity and further reduced peptide inhibitory potency. It is concluded that S138A increased binding of HR2/ENF into grooves and that S138A compensated for electrostatic repulsion between N43D and HR2. The six-helix bundle structure indicated that E148A should increase hydrophobic interactions between the coiled-coil and peptide. Importantly, the modifications S138A and E148A in the same peptide retained potency against ENF-escape mutants. The double mutant's increase in potency was greater than the increases from the sum of S138A and E148A individually, showing that these two altered residues synergistically contributed to peptide binding. Isothermal titration calorimetry established that hydrophobic substitutions at positions S138 and E148 improved potency of inhibitory peptides against escape mutants by increasing enthalpic release of energy upon peptide binding." @default.
• W2069401811 created "2016-06-24" @default.
• W2069401811 creator A5052874208 @default.
• W2069401811 creator A5082925246 @default.
• W2069401811 date "2011-04-01" @default.
• W2069401811 modified "2023-09-26" @default.
• W2069401811 title "Increasing Hydrophobicity of Residues in an Anti-HIV-1 Env Peptide Synergistically Improves Potency" @default.
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• W2069401811 doi "https://doi.org/10.1016/j.bpj.2011.02.053" @default.
• W2069401811 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3077694" @default.
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