Evaluating interaction forces between BSA and rabbit anti-BSA in sulphathiazole sodium, tylosin and levofloxacin solutio
- PDF / 479,367 Bytes
- 9 Pages / 595.28 x 793.7 pts Page_size
- 56 Downloads / 166 Views
NANO EXPRESS
Open Access
Evaluating interaction forces between BSA and rabbit anti-BSA in sulphathiazole sodium, tylosin and levofloxacin solution by AFM Congzhou Wang1,2, Jianhua Wang1,2* and Linhong Deng1,2
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. 1. Introduction A molecular level understanding of protein-protein interactions is fundamentally important in the life sciences. A number of human diseases are closely related to the protein-protein association or dissociation events and thus probing and characterizing these interactions have become increasingly significant in the development of novel drugs and medical diagnostics [1-4]. Different solution conditions, such as pH, temperature, ion species, and strength, may influence the protein-protein interactions as previous studies have demonstrated [5-7]. This is particularly important in drug discovery and the computer-aided drug design (CADD) method has identified molecules modifying protein-protein interactions as potential drug candidates [8,9]. However, the computer studies do not provide more detailed information on forces at nanoscale-to-molecular scale that influence protein-protein interactions, which would allow us to better understanding the factors of drug molecules affecting the interactions. Therefore, it * Correspondence: [email protected] 1 Key Laboratory of Biorheological Science and Technology, Ministry of Education, Chongqing University, 400044 Chongqing, China Full list of author information is available at the end of the article
is still challenging to evaluate the protein-protein interactions, such as that between antigen and antibody, in the presence of drug molecules in physiological liquid. Bovine serum albumin (BSA) is the major protein constit
Data Loading...
