Peptides Design Based on the Interfacial Helix of Integrase Dimer

HIV-I integrase (IN) plays a crucial role in the retroviral life cycle. The peptides derived from the helix of IN were reported to have the potency of inhibition. We designed a series of peptides based on interface helices alpha1 and alpha5 with the aim of increasing their inhibitory activity. The helix-forming tendency and the affinity with IN were essential for interfacial peptide inhibitors. The MD simulation and AGADIR prediction both showed favorable results for the designed peptides. The binding mode and binding free energy of peptide and IN were investigated subsequently to test our design. The improvement in binding free energy compared with that of alpha1 and alpha5 indicates that some of the designed peptides may have a higher potency for inhibiting the dimerization of IN. This study provides some useful information for rational design of IN peptide inhibitor