Document Detail

Insight into the modified Ibalizumab-human CD4 receptor interactions: using a computational binding free energy approach.
MedLine Citation:
PMID:  25342515     Owner:  NLM     Status:  Publisher    
Antibody drugs are very useful tools for the treatment of many chronic diseases. Recently, however, patients and doctors have encountered the problem of drug resistance. How to improve the affinity of antibody drugs has therefore become a pressing issue. Ibalizumab is a humanized monoclonal antibody that binds human CD4, the primary receptor for human immunodeficiency virus type 1. This study investigates the mutation residues of the complementarity determining regions of Ibalizumab. We propose using the wild and mutations of Ibalizumab-human CD4 receptor complex structures, molecular dynamics techniques, alanine-scanning mutagenesis calculations and solvated interaction energies methods to predict the binding free energy of the Ibalizumab-human CD4 receptor complex structures. This work found that revealed three key positions (31th, 32th and 33th in HCDR-1) of the residues may play an important role in Ibalizumab-human CD4 receptor complex interactions. Therefore, bioengineering substitutions of the three key positions and increasing number of intermolecular interactions (HCDR-1 of Ibalizumab/human CD4 receptor) might improve the binding affinities of this complex structure.
Yeng-Tseng Wang; Lea-Yea Chuang
Related Documents :
8277945 - Relationship between zinc content and dna-binding activity of the dna-binding motif of ...
14559915 - Identification of a secondary zinc-binding site in staphylococcal enterotoxin c2. impli...
25186975 - Long-range stabilization of anthrax protective antigen upon binding to cmg2.
3208745 - Footprinting of linker histones h5 and h1 on the nucleosome.
10593515 - The murine clan v(h) iii related 7183, j606 and s107 and dna4 families commonly encode ...
8395515 - Detergent binding as a measure of hydrophobic surface area of integral membrane proteins.
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-10-24
Journal Detail:
Title:  Journal of computer-aided molecular design     Volume:  -     ISSN:  1573-4951     ISO Abbreviation:  J. Comput. Aided Mol. Des.     Publication Date:  2014 Oct 
Date Detail:
Created Date:  2014-10-24     Completed Date:  -     Revised Date:  2014-10-25    
Medline Journal Info:
Nlm Unique ID:  8710425     Medline TA:  J Comput Aided Mol Des     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms

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

Previous Document:  An Internet-Based Ecological Momentary Assessment Study Relying on Participants' Own Mobile Phones: ...
Next Document:  Stereotactic radiotherapy for isolated nodal recurrence of prostate cancer.