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• W2068293804 abstract "In this study, we present the first account of pentacycloundecane (PCU) peptide based HIV-protease inhibitors. The inhibitor exhibiting the highest activity made use of a natural HIV-protease substrate peptide sequence, that is, attached to the cage (PCU–EAIS). This compound showed nanomolar IC 50 activity against the resistance-prone wild type C-South African HIV-protease (C-SA) catalytic site via a norstatine type functional group of the PCU hydroxy lactam. NMR was employed to determine a logical correlation between the inhibitory concentration (IC 50 ) results and the 3D structure of the corresponding inhibitors in solution. NMR investigations indicated that the activity is related to the chirality of the PCU moiety and its ability to induce conformations of the coupled peptide side chain. The results from docking experiments coincided with the experimental observed activities. These findings open up useful applications for this family of cage peptide inhibitors, considering the vast number of alternative disease related proteases that exist." @default.
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• W2068293804 date "2011-04-01" @default.
• W2068293804 modified "2023-09-26" @default.
• W2068293804 title "Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease" @default.
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• W2068293804 doi "https://doi.org/10.1016/j.bmcl.2011.02.105" @default.
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