Abstract
Three synthetic oligopeptides (EAA26, K156 and E156) mutant of the α-4 helix of the HIV-1 integrase and having, respectively, 26, 24 and 24 aminoacids showed variable oligomerisation trend as detected by the ESI-MS (electrospray mass spectrometry) or CD (circular dichroism) methodologies. These peptides oligomers were modelled as potential inhibitors of this enzyme through coiled–coil interactions. The dimer, trimer and tetramer aggregate energies for these synthetic peptides were calculated and their stability discussed. One of these peptides, EAA26 shows some propensity to form a tetrameric structure when attached to the calix[4]arene frame through a succinic linker; the possibility to form the quadruple peptide helix, an entity which was not obtained from peptide systems, was evaluated.
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