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https://ir.swu.ac.th/jspui/handle/123456789/15096| Title: | Particular interaction between efavirenz and the HIV-1 reverse transcriptase binding site as explained by the ONIOM2 method |
| Authors: | Nunrium P. Kuno M. Saen-Oon S. Hannongbua S. |
| Keywords: | Aromatic compounds Binding energy Conformations Crystal structure Enzyme inhibition Hydrogen bonds Quantum theory Viruses X ray analysis Drug resistance Efavirenz Non-neucleoside inhibitor binding pockets (NNIBP) X-ray structure Drug products |
| Issue Date: | 2005 |
| Abstract: | Particular interaction between efavirenz and the HIV-1 reverse transcriptase binding site was investigated, based on the B3LYP/6-31G(d,p) and ONIOM2 methods. The interaction between efavirenz and Lys101 was found to be the strongest interaction, typically, -11.29 kcal/mol. The stability of this complex system leads to the foundation of the estimated binding energy of approximately -22.66 kcal/mol. Moreover, two hydrogen bonds between benzoxazin-2-one, and the backbone carbonyl oxygen and the backbone amino hydrogen of Lys101 were observed. These hydrogen bond interactions play an important role in the bound efavirenz/HIV-1 RT complex. © 2005 Elsevier B.V. All rights reserved. |
| URI: | https://ir.swu.ac.th/jspui/handle/123456789/15096 https://www.scopus.com/inward/record.uri?eid=2-s2.0-16244380541&doi=10.1016%2fj.cplett.2005.02.023&partnerID=40&md5=de8f5122b53d88a6bc64bc0f7ed1f31e |
| ISSN: | 92614 |
| Appears in Collections: | Scopus 1983-2021 |
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