Potential of mean force of the hepatitis C virus core protein–monoclonal 19D9D6 antibody interaction |
| |
Authors: | Yeng-Tseng Wang Zhi-Yuan Su Cheng-Lung Chen |
| |
Affiliation: | aNational Center for High-performance Computing, Hsin-Shi, Tainan County, Taiwan;bThe Department of Chemistry, National Sun Yat-Sen University, Kaohsiung 804, Taiwan;cThe Department of Information Management, Chia Nan University of Pharmacy and Science, Tainan 717, Taiwan |
| |
Abstract: | Antigen–antibody interactions are critical for understanding antigen–antibody associations in immunology. To shed further light on this question, we studied a dissociation of the 19D9D6-HCV core protein antibody complex structure. However, forced separations in single molecule experiments are difficult, and therefore molecular simulation techniques were applied in our study. The stretching, that is, the distance between the center of mass of the HCV core protein and the 19D9D6 antibody, has been studied using the potential of mean force calculations based on molecular dynamics and the explicit water model. Our simulations indicate that the 7 residues Gly70, Gly72, Gly134, Gly158, Glu219, Gln221 and Tyr314, the interaction region (antibody), and the 14 interprotein molecular hydrogen bonds might play important roles in the antigen–antibody interaction, and this finding may be useful for protein engineering of this antigen–antibody structure. In addition, the 3 residues Gly134, Gly158 and Tyr314 might be more important in the development of bioactive antibody analogs. |
| |
Keywords: | Molecular dynamics Potential of mean force Hepatitis C virus Antibody |
本文献已被 ScienceDirect 等数据库收录! |
|