Document Detail


Study on the molecular mechanism of inhibiting HIV-1 integrase by EBR28 peptide via molecular modeling approach.
MedLine Citation:
PMID:  18037557     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human immunodeficiency virus type 1 (HIV-1) integrase (IN) is an essential enzyme in the HIV-1 lifecycle which aids the integration of viral DNA into the host chromosome. Recently synthesized 12-mer peptide EBR28, which can strongly bind to IN, is one of the most potential small peptide leading compounds inhibiting IN binding with viral DNA. However, the binding mode between EBR28 peptide with HIV-1 IN and the inhibition mechanism remain uncertain. In this paper, the binding modes of EBR28 with HIV-1 IN monomer core domain (IN(1)) and dimmer core domain (IN(2)) were investigated by using molecular docking and molecular dynamics (MD) simulation methods. The results indicated that EBR28 bound to the interfaces of the IN(1) and IN(2) systems mainly through the hydrophobic interactions with the beta3, alpha1 and alpha5 regions of the proteins. The binding free energies for IN(1) with a series of EBR28 mutated peptides were calculated with the MM/GBSA model, and the correlation between the calculated and experimental binding free energies is very good (r=0.88). Thus, the validity of the binding mode of IN(1) with EBR28 was confirmed. Based on the binding modes, the inhibition mechanism of EBR28 was explored by analyzing the essential dynamics (ED), energy decomposition and the mobility of EBR28 in the two docked complexes. The proposed inhibition mechanism is represented that EBR28 binds to the interface of IN(1) to form the IN(1)_EBR28 complex and preventes the formation of IN dimmer, finally leads to the partial loss of binding potency for IN with viral DNA. All of the above simulation results agree well with experimental data, which provide us with some helpful information for designing anti-HIV small peptide drugs.
Authors:
Jian Ping Hu; Xin Qi Gong; Ji Guo Su; Wei Zu Chen; Cun Xin Wang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-09-29
Journal Detail:
Title:  Biophysical chemistry     Volume:  132     ISSN:  0301-4622     ISO Abbreviation:  Biophys. Chem.     Publication Date:  2008 Feb 
Date Detail:
Created Date:  2007-12-20     Completed Date:  2008-04-17     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0403171     Medline TA:  Biophys Chem     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  69-80     Citation Subset:  IM    
Affiliation:
College of Life Science and Bioengineering, Beijing University of Technology, Beijing, China.
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Computer Simulation
HIV Integrase / chemistry*
HIV Integrase Inhibitors / chemistry*
HIV-1 / enzymology*
Humans
Models, Chemical*
Oligopeptides / chemistry*
Protein Binding
Chemical
Reg. No./Substance:
0/EBR28 peptide; 0/HIV Integrase Inhibitors; 0/Oligopeptides; EC 2.7.7.-/HIV Integrase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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