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- W96237092 abstract "Since the first discovery that cross-linked peptides corresponding to the dimerization interface of HIV-1 PR (1) can effectively inhibit the formation of the active homodimer of HIV-1 protease [1], extensive work to improve upon this class of inhibitors has been done leading to smaller inhibitors such as 2. In the absence of structural data, questions of the binding locus of each peptide remain. Do the peptides bind differentially and would the use of identical peptides cross-linked to mimic the dimerization interface be more beneficial than a more tedious synthesis of differentially substituted inhibitors? To answer these questions and to gain further insight into the use of dimerization inhibitors a series of Identically Substituted Cross-linked Protease Inhibitors (ISCPIs) were synthesized and evaluated against Non-Identical Cross-linked Protease Inhibitors (NISCPIs). In all of the cases investigated (17) except for one, all ISCPIs were less potent than their corresponding NISCPIs. The one exception yielded a compound with similar potency as judged by the value, but one that did not inhibit HIV-1 PR through a dissociative mechanism." @default.
- W96237092 created "2016-06-24" @default.
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- W96237092 date "2006-05-16" @default.
- W96237092 modified "2023-09-26" @default.
- W96237092 title "Dimerization inhibitors of HIV-1 protease: Effective inhibition requires the cross-linking of non-identical peptides" @default.
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- W96237092 doi "https://doi.org/10.1007/0-306-46881-6_6" @default.
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