|
|||||
|
|
Theoretical investigation on the binding specificity of fluorinated sialyldisaccharides Neu5Acα(2–3)Gal and Neu5Acα(2–6)Gal with influenza hemagglutinin H1 – A Molecular Dynamics Study |
|
| Authors: | Veeramani Murugan Ponnusamy Parasuraman Jeyasigamani F A Selvin Michael M Gromiha Kazuhiko Fukui |
| Institution: | 1. Department of Physics, Manonmaniam Sundaranar University, Tirunelveli, Tamilnadu, India;2. Department of Physical Sciences, Bannari Amman Institute of Technology, Erode, Tamilnadu, India;3. Department of Physics, NMSSVN College, Madurai, Tamilnadu, India;4. Department of Biotechnology, Indian Institute of Technology Madras, Chennai, Tamilnadu, India;5. National Institute of Advanced Industrial Science and Technology (AIST), Molecular Profiling Research Center for Drug Discovery (molprof), 2-4-7 Aomi, Koto-ku, Tokyo, Japan |
| Abstract: | In the present study, the hydroxyl groups at the C4 and C7 positions of sialic acid and C6 position of galactose in Neu5Acα(2–3)Gal (N23G) and the hydroxyl groups at the C8 position of sialic acid and C3 and C4 positions of galactose in Neu5Acα(2–6)Gal (N26G) were substituted with fluorine atoms, respectively. Molecular dynamics simulations of 100 ns duration were carried out to investigate the structural and dynamical behavior of H1 bound with the tri-fluorinated N23G and N26G (FN23G and FN26G). Based on energy analysis, it was concluded that FN26G should be a better binder for hemagglutinin (H1) than FN23G and it might act as an inhibitor for influenza. |
| Keywords: | fluorinated sialyldisaccharide molecular dynamics hemagglutinin binding specificity influenza A virus inhibitor design |