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. 2010 Jul 21;107(32):14093–14098. doi: 10.1073/pnas.1002713107

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Fig. 3. — Enhanced antiviral activity of SAH-gp41_(626–662)(A, B). (A) The gp41 HR2-derived peptides all blocked HXBc2 infectivity, with the T649v-based constructs showing slightly superior activity compared to enfuvirtide. (B) Singly and doubly stapled SAH-gp41_(626–662) peptides demonstrated enhanced blockade of a neutralization-resistant virus that contains the YU2 envelope glycoproteins, with SAH-gp41_(626–662)(A, B) exhibiting the most potent antiviral activity. SAH-gp41_(626–662)(A, B) outperformed enfuvirtide and T649v in HR1/HR2 complex assembly (C, D) and infectivity assays (E, F) that respectively employed peptides and recombinant HIV-1 constructs bearing HR1 enfuvirtide-resistance mutations. % viral infection, mean ± s.e.m; IC50, mean ± s.d.