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Pavinee Prapassornwattana. Theoretical study of effect on mutation at the surface of viral capsid of coxsackievirus B3 on the binding of a benzene sulfonamide derivative. Master's Degree(Chemistry). Kasetsart University. Office of the University Library. : Kasetsart University, 2021.
Theoretical study of effect on mutation at the surface of viral capsid of coxsackievirus B3 on the binding of a benzene sulfonamide derivative
Classification :.LCCS: QD341.H9
LCSH:
Benzenesulfonamide
LCSH:
Sulfonamides
LCSH:
Coxsackieviruses
LCSH:
Picornaviruses
LCSH:
Enteroviruses
Abstract:
Coxsackievirus B3 (CVB3) is one of serotypes in family picornaviridae. CVB3 was an outbreak in worldwide from 1983 to 2016. In Thailand, CVB3 was found as the majority of the identified clinical samples of viral pathogens between 2008 and 2011. CVB3 could cause many diseases including hand, foot and mouth disease (HFMD), pericarditis, myocarditis, etc. CVB3 used the viral capsid proteins to interact with the host-cell receptors. The viral capsid proteins (VPs) of CVB3 consist of 4 chains including VP1, VP2, VP3, and VP4. Recently, the novel druggable pocket of CVB3 was reported at VP1 and VP3 of CVB3. The structure of a benzene sulfonamide derivative (compound 1) was reported that compound 1 was a new target for viral capsid proteins (VPs) of CVB3. In order to examine which form of compound 1 could inhibit well with the CVB3 monomer. The neutral and ionized forms of compound 1 binding with the CVB3 monomer were studied by using molecular dynamics (MD) simulations, quantum mechanics (QM) calculations, and quantum mechanics and molecular mechanics (QM/MM) calculations After that, the extended VP1 chain was added in the study in order to cover all the binding pocket called as dimer, were also applied to study the binding with the compound 1. The binding of compound 1 with wild-type (WT) and some mutant VPs of CVB3. The results revealed that the ionized form of compound 1 could bind better than its neutral form. From the dimer systems, VP1:Arg234 and VP1:Arg219 are key residues for the binding. The insight interaction could also explain why the compound 1 could still inhibit some mutants of CVB3. The obtained results will be useful for the development of CVB3 drugs.
Kasetsart University. Office of the University Library
Address:
Bangkok
Email:
tdckulib@ku.ac.th
Name: Patchreenart Saparpakorn
Role:
Thesis Advisor
Name: Supa Hannongbua
Role:
Thesis CO-Advisor
Created:
2021
Modified:
2025-07-24
Issued:
2025-07-24
วิทยานิพนธ์/Thesis
application/pdf
URL: https://www.lib.ku.ac.th/KUthesis/2564/pavinee-pra-all.pdf
CallNumber:
QD341.H9 .P38
eng
DegreeName: Master of Science
Level: Master's Degree
Descipline: Chemistry
Grantor: Kasetsart University
©copyrights Kasetsart University
RightsAccess:
ใช้เวลา
0.024994 วินาที
Pavinee Prapassornwattana
| Title | Contributor | Type |
|---|---|---|
| Theoretical study of effect on mutation at the surface of viral capsid of coxsackievirus B3 on the binding of a benzene sulfonamide derivative
มหาวิทยาลัยเกษตรศาสตร์ Pavinee Prapassornwattana | Patchreenart Saparpakorn | วิทยานิพนธ์/Thesis |
Patchreenart Saparpakorn
Supa Hannongbua