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Publikasi Scopus 2010 s/d 2022
Publikasi Scopus 2010 s/d 2022
Prediction of MMP-9 Polymorphism Impacts on MDR-TB by Molecular Simulation and Network Interaction
2022
Pharmacognosy Journal
14
6
833
841
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85159798959&doi=10.5530%2fpj.2022.14.176&partnerID=40&md5=c6b1cde4f74725f2d360ecc830022cb0
Doctoral Program in Biomedical Sciences, Faculty of Medicine University of Indonesia, Indonesia; Department of Radiology, General Hospital Cipto Mangunkusumo, Faculty of Medicine University of Indonesia, Indonesia; Department of Internal Medicine Sciences, Pulmonology division, Faculty of Medicine, University of Indonesia, Indonesia; Department of Pulmonology, General Hospital Abdoel Moelok, Faculty of Medicine University of Lampung, Indonesia; Department of Community Medical Sciences, Faculty University of Indonesia Medicine, Indonesia; Departement of Medical Biology, Faculty of Medicine Universitas Indonesia, Jakarta, Indonesia; Departement of Medical Chemistry, Faculty of Medicine Universitas Indoensia, Jakarta, Indonesia; Bioinformatics Core Facilities - IMERI, Faculty of Medicine, Universitas Indonesia, Jakarta, Indonesia
MMP-9 overexpression is associated with a poor outcome in MDR-TB patients, indicating that MMP-9 is a suitable target for MDR-TB therapy. MMP-9 also includes SNPs that occur at inhibitor binding areas as well as zinc ions. As a result of polymorphisms, the usage of MMP-9 inhibitors for MDR-TB might vary. Through molecular simulation, it has been found that the mutant MMP-9 has a larger cavity and a more lipophilic surface. The docking tests revealed that EGTA had the least amount of binding energy to both wild-type and mutant MMP-9. The wildtype MMP-9 can bind zinc when EGTA is in the active site. This shows that using EGTA to chelate Zn is only partially successful. However, the binding energy of EGTA at the active site suggests that it may be a competitor to MMP-9 substrates. On the other hand, Zn is not involved in the interaction of the mutant MMP-9-EGTA complex. © 2022 Phcogj.Com.
gelatinase B; metalloproteinase inhibitor; adult; Article; controlled study; gene overexpression; genetic association; genetic polymorphism; human; lipophilicity; molecular docking; multidrug resistant tuberculosis; outcome assessment; prediction; protein expression; simulation; single nucleotide polymorphism; wild type
Universitas Indonesia
We are thankful to all authors who provided expertise that greatly assisted the research. This work was supported by Universitas Indonesia grant for International Indexed Publication (PUTI) Doctoral with Number: NKB-571/UN2.RST/HKP.05.00/2020.
EManuscript Technologies
09753575
Article
Q3
258
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