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Evaluating interaction forces between BSA and rabbit anti-BSA in sulphathiazole sodium, tylosin and levofloxacin solution by AFM

Wang, Congzhou and Wang, Jianhua and Deng, Linhong (2011) Evaluating interaction forces between BSA and rabbit anti-BSA in sulphathiazole sodium, tylosin and levofloxacin solution by AFM. NANOSCALE RESEARCH LETTERS, 6 (1). pp. 1-9. ISSN 1931-7573 (Print) 1556-276X (Online)

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Official URL: http://www.nanoscalereslett.com/content/6/1/579

Abstract

Protein-protein interactions play crucial roles in numerous biological processes. However, it is still challenging to evaluate the protein-protein interactions, such as antigen and antibody, in the presence of drug molecules in physiological liquid. In this study, the interaction between bovine serum albumin (BSA) and rabbit anti-BSA was investigated using atomic force microscopy (AFM) in the presence of various antimicrobial drugs (sulphathiazole sodium, tylosin and levofloxacin) under physiological condition. The results show that increasing the concentration of tylosin decreased the single-molecule-specific force between BSA and rabbit anti-BSA. As for sulphathiazole sodium, it dramatically decreased the specific force at a certain critical concentration, but increased the nonspecific force as its concentration increasing. In addition, the presence of levofloxacin did not greatly influence either the specific or nonspecific force. Collectively, these results suggest that these three drugs may adopt different mechanisms to affect the interaction force between BSA and rabbit anti-BSA. These findings may enhance our understanding of antigen/antibody binding processes in the presence of drug molecules, and hence indicate that AFM could be helpful in the design and screening of drugs-modulating protein-protein interaction processes.

Item Type:Article
Subjects:Analytical Science > Microscopy and probe methods
Biomedical Science > Nanotechnology for animal health
ID Code:11579
Deposited By:M T V
Deposited On:05 Jan 2012 11:00
Last Modified:05 Jan 2012 11:00

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