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Molecular and Electronic Properties of HIV-1 Protease Inhibitor C
60
derivatives asStudied by the ONIOM Method
 
Siriporn Promsri
1
, Parawan Chuichay
1
, Vannajan Sanghiran
2
, Vudhichai Parasuk 
1
,Supot Hannongbua
1,*
 
1
 Department of Chemistry, Faculty of Science, Chulalongkorn University, Bangkok, 10330Thailand.
2
Department of Chemistry, Faculty of Science, Chiangmai University, Chiangmai, Thailand.
 
TOTAL PAGE 17TOTAL TABLES 1TOTAL FIGURES 6*
To whom correspondence should be addressed. Email: supot.h@chula.ac.th
 
 
Abstract
Quantum chemical methods were performed to study the structure and electronic properties of a series of C
60
derivatives. The integrated, ONIOM molecular orbital methodwas applied to optimize the structure of all compounds while the DFT/ B3LYP 6-31G(d)calculations were performed to examine molecular and electronic properties. It was foundthat strongest effect of the functional groups on the net charges takes place on the linkedatoms between C
60
and its side chain. The functional group leads to the changes of atomic netcharges on the C
60
surface up to 5 Å away from the C—C bond where the functional group binds to the surface. Two localized electrostatic potential regions are observed, for theselected compounds, near the hydroxyl oxygen and the hydroxyl hydrogen. The hydroxylhydrogen atom is the location of the most positive potential. These electrostatic features arelikely modulated the hydrophobicity or lipophilicity of the compounds and, hence, indicatehow they interact with the receptor.
 
 
1. Introduction
HIV protease (HIV PR) is one of the most intensely studied aspartic peptidase, neededfor viral replication implicated in AIDS, during the last 20 years [1]. It was found that water 
-
soluble methanofullerene derivative was a competitive inhibitor for this purpose [2, 3].
 
Therefore, various sizes of fullerene derivatives have been synthesized and their biologicalactivities have been widely measured and reported [4-8]. On the basis of molecular modeling, Friedman et. al.
 
[2]
 
anticipated that a C
60
 
molecule fits nicely into the hydrophobiccavity of the protease specific for HIV-1 because of the steric bulk of C
60
 
and itscomplementarity to the active site surface of HIV-PR.
 
The core fullerene moiety wasobserved to bind snugly into the active
 
site. It was confirmed experimentally that the bindingaffinity of C
60
derivatives is in the low-micromolar to nanomolar range [3]. In addition, themain mechanism of action of these derivatives is hydrophobic interaction.It is known that binding of drug to HIV
-
1 protease alters their physicochemical properties and the potency of binding correlates with the hydrophobicity of the drug.
 
Therefore, understanding of the structural and the electrostatic features of these compoundswould lead directly to an understanding of the mechanism of their action [9]. As receptor recognized stereo
-
electronic effects, studies of molecular and electronic properties by meansof quantum chemical calculations could also provide essential information in the field of structure based drug design.The present study is an assessment of structural features and electronic propertiestoward an improved understanding of the structure
-
activity relationship of C
60
derivatives toenable a prediction of potent antiviral activity.
 
The study encompassed 10
 
compounds asshown in Figure 1.
 
Optimizations have been made using the Own N
-
layered Integratedmolecular Orbital and molecular Mechanics or ONIOM algorithm [10-12].
 
The ONIOMscheme allows treating a selected area of a large system at a high level, whereas the rest of the system is treated using a computationally more feasible level of theory. Analyses of electrostatic potentials (ESP) and molecular properties have been investigated in detail.
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