Structure-activity relationship study of some inhibitors of HIV-1 integrase

Recently a new and simple methodology has been proposed to correlate electronic indices to the biological activity of a class of carcinogenic polycyclic aromatic hydrocarbons (PAHs). This methodology was based on the energy separation values between frontier orbitals and in their relative contribution to the local density of electronic states over specific molecular regions. In this work we adapted the methodology to the study of some new HIV-1 Integrase inhibitors. Integrase is an HIV-1 enzyme essential for effective viral replication Our calculations were carried out using the semi-empirical Parametric Method 3 (PM3). Our results show that, similar to the PAHs, it is possible to derive very simple rules correlating inhibitory integrase activity to electronic indices. (C) 1999 Published by Elsevier Science Ltd. All rights reserved.Recently a new and simple methodology has been proposed to correlate electronic indices to the biological activity of a class of carcinogenic polycyclic aromatic hydrocarbons (PAHs). This methodology was based on the energy separation values between frontier orbitals and in their relative contribution to the local density of electronic states over specific molecular regions. In this work we adapted the methodology to the study of some new HIV-1 Integrase inhibitors. Integrase is an HIV-1 enzyme essential for effective viral replication Our calculations were carried out using the semi-empirical Parametric Method 3 (PM3). Our results show that, similar to the PAHs, it is possible to derive very simple rules correlating inhibitory integrase activity to electronic indices. (C) 1999 Published by Elsevier Science Ltd. All rights reserved.