Antibody-Ligand Interactions: Computational Modeli ng and Correlation with Biophysical Measurements

Authors: Linthicum D.S.; Tetin S.Y.; Anchin J.M.; Loerger T.R.

Source: Combinatorial Chemistry & High Throughput Screening, Volume 4, Number 5, August 2001 , pp. 439-449(11)

Publisher: Bentham Science Publishers

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Abstract:

Several new aspects of computer-assisted molecular modeling strategies and biophysical techniques, such as fluorescence spectroscopy, circular dichroism, and absorption spectroscopy, have proved useful in the analysis and description of antibody-ligand interactions. The molecular features involved in determining the specificity of antibody-ligand interactions, such as electrostatics (e.g. partial charges, salt bridges, pi-cation motifs), hydrogen-bonds, polarization, hydrophobic interactions, hydration and solvation effects, entropy, and kinetics can be identified using a battery of biophysical techniques. An understanding of these parameters is essential to our use of antibodies as tools in high throughput screening of chemical libraries for the discovery of novel compounds.

Keywords: antibody ligand interactions; radiommunoassay ria enzyme immunoassay eia; equilibrium dialysis ria; computer assisted molecular modeling camm

Language: English

Document Type: Review article

DOI: 10.2174/1386207013330995

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