A systematic evaluation of the inhibition of HIV-1 protease by its C- and N-terminal peptides
C- and N-terminal peptides of varying lengths corresponding to the dimerization interface of the retroviral protease of the human immunodeficiency virus-1 (HIV-1 protease) have been synthesized and evaluated as inhibitors of HIV-1 protease activity.
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Design, synthesis and structure-activity study of shorter hexa peptide analogues as HIV-1 protease inhibitors
2008, Bioorganic and Medicinal ChemistryThyroxine-derivatives of lipopeptides: Bifunctional dimerization inhibitors of human immunodeficiency virus-1 protease
2003, Biochemical PharmacologyCitation Excerpt :In both cases, the interface region which displays large hydrophobic pockets (Fig. 3B) may be more accessible to ANS. Lipopeptides are the best of known dimerization inhibitors when compared to cross-linked interface peptides (Kid=220 nM [12,13], 780 nM [19]) and conformationally constrained hairpins (Kid=560 nM [15], 5400 nM [16]). This study shows that: (i) the further amino acid elongation of the Pam-tripeptides is not necessary to enhance dimerization inhibitory efficiency; (ii) the binding pocket for the third C-terminal amino acid in 3-mer lipopeptides is hydrophobic and large enough to accommodate a variety of groups, confirming computer design [10,27].
HIV protease as a target for retrovirus vector-mediated gene therapy
2000, Biochimica et Biophysica Acta - Protein Structure and Molecular EnzymologyRestricting the flexibility of crosslinked, interfacial peptide inhibitors of HIV-1 protease
1998, Bioorganic and Medicinal Chemistry LettersHydrophobicity versus activity in crosslinked interfacial peptide inhibitors of HIV-1 protease
1997, Tetrahedron AsymmetryThe inhibition of human immunodeficiency virus proteases by 'interface peptides'
1996, Antiviral Research