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Improved scFv Anti-HIV-1 p17 Binding Affinity Guided from the Theoretical Calculation of Pairwise Decomposition Energies and Computational Alanine Scanning
Joint Authors
Zain, S. M.
Tue-ngeun, Panthip
Kodchakorn, Kanchanok
Nimmanpipug, Piyarat
Lawan, Narin
Nangola, Sawitree
Tayapiwatana, Chatchai
Lee, Vannajan Sanghiran
Abd Rahman, Noorsaadah
Source
Issue
Vol. 2013, Issue 2013 (31 Dec. 2013), pp.1-12, 12 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2013-11-07
Country of Publication
Egypt
No. of Pages
12
Main Subjects
Abstract EN
Computational approaches have been used to evaluate and define important residues for protein-protein interactions, especially antigen-antibody complexes.
In our previous study, pairwise decomposition of residue interaction energies of single chain Fv with HIV-1 p17 epitope variants has indicated the key specific residues in the complementary determining regions (CDRs) of scFv anti-p17.
In this present investigation in order to determine whether a specific side chain group of residue in CDRs plays an important role in bioactivity, computational alanine scanning has been applied.
Molecular dynamics simulations were done with several complexes of original scFv anti-p17 and scFv anti-p17mutants with HIV-1 p17 epitope variants with a production run up to 10 ns.
With the combination of pairwise decomposition residue interaction and alanine scanning calculations, the point mutation has been initially selected at the position MET100 to improve the residue binding affinity.
The calculated docking interaction energy between a single mutation from methionine to either arginine or glycine has shown the improved binding affinity, contributed from the electrostatic interaction with the negative favorably interaction energy, compared to the wild type.
Theoretical calculations agreed well with the results from the peptide ELISA results.
American Psychological Association (APA)
Tue-ngeun, Panthip& Kodchakorn, Kanchanok& Nimmanpipug, Piyarat& Lawan, Narin& Nangola, Sawitree& Tayapiwatana, Chatchai…[et al.]. 2013. Improved scFv Anti-HIV-1 p17 Binding Affinity Guided from the Theoretical Calculation of Pairwise Decomposition Energies and Computational Alanine Scanning. BioMed Research International،Vol. 2013, no. 2013, pp.1-12.
https://search.emarefa.net/detail/BIM-1030826
Modern Language Association (MLA)
Tue-ngeun, Panthip…[et al.]. Improved scFv Anti-HIV-1 p17 Binding Affinity Guided from the Theoretical Calculation of Pairwise Decomposition Energies and Computational Alanine Scanning. BioMed Research International No. 2013 (2013), pp.1-12.
https://search.emarefa.net/detail/BIM-1030826
American Medical Association (AMA)
Tue-ngeun, Panthip& Kodchakorn, Kanchanok& Nimmanpipug, Piyarat& Lawan, Narin& Nangola, Sawitree& Tayapiwatana, Chatchai…[et al.]. Improved scFv Anti-HIV-1 p17 Binding Affinity Guided from the Theoretical Calculation of Pairwise Decomposition Energies and Computational Alanine Scanning. BioMed Research International. 2013. Vol. 2013, no. 2013, pp.1-12.
https://search.emarefa.net/detail/BIM-1030826
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1030826