Study of peptide oligomer derived from HIV-1 integrase molecular modelling

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.