By a News Reporter-Staff News Editor at Life Science Weekly -- Research findings on Immunology are discussed in a new report. According to news reporting originating in Hangzhou, People's Republic of China, by NewsRx journalists, research stated, "Affinity chromatography with synthetic ligands has been focused as the potential alternative to protein A-based chromatography for antibody capture because of its comparable selectivity and efficiency. Better understanding on the molecular interactions between synthetic ligand and antibody is crucial for improving and designing novel ligands."
The news reporters obtained a quote from the research from Zhejiang University, "In this work, the molecular interaction mechanism between Fc fragment of IgG and a synthetic ligand (DAAG) was studied with molecular docking and dynamics simulation. The docking results on the consensus binding site (CBS) indicated that DAAG could bind to the CBS with the favorable orientation like a tripod for the top-ranked binding complexes. The ligand-Fc fragment complexes were then tested by molecular dynamics simulation at neutral condition (pH7.0) for 10ns. The results indicated that the binding of DAAG on the CBS of Fc fragment was achieved by the multimodal interactions, combining the hydrophobic interaction, electrostatic interaction, hydrogen bond, and so on. It was also found that multiple secondary interactions endowed DAAG with an excellent selectivity to Fc fragment. In addition, molecular dynamics simulation conducted at acidic condition (pH3.0) showed that the departure of DAAG ligand from the surface of Fc fragment was the result of reduced interaction energies."
According to the news reporters, the research concluded: "The binding modes between DAAG and CBS not only shed light on the molecular mechanisms of DAAG for antibody purification but also provide useful information for the improvement of ligand design."
For more information on this research see: Molecular insights into the binding selectivity of a synthetic ligand DAAG to Fc fragment of IgG. Journal of Molecular Recognition, 2014;27(5):250-259. Journal of Molecular Recognition can be contacted at: Wiley-Blackwell, 111 River St, Hoboken 07030-5774, NJ, USA. (Wiley-Blackwell - www.wiley.com/; Journal of Molecular Recognition - onlinelibrary.wiley.com/journal/10.1002/(ISSN)1099-1352)
Our news correspondents report that additional information may be obtained by contacting R.Z. Wang, Zhejiang University, Dept. of Chem & Biol Engn, Key Lab Biomass Chem Engn, Minist Educ, Hangzhou 310027, Zhejiang, People's Republic of China. Additional authors for this research include D.Q. Lin, H.F. Tong and S.J. Yao (see also Immunology).
Keywords for this news article include: Asia, Antibodies, Physics, Hangzhou, Immunology, Blood Proteins, Immunoglobulins, Molecular Dynamics, People's Republic of China
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