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All Journal The Journal of Pure and Applied Chemistry Research
Fatchiyah Fatchiyah
1Department of Biology, Faculty of Mathematics and Sciences, Brawijaya University, Indonesia 2Research Center of Smart Molecule and Natural Genetic Resources, Brawijaya University, Indonesia
Chemical Engineering, Chemistry & Bioengineering Chemistry Materials Science & Nanotechnology Medicine & Pharmacology

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The Biological Function Prediction of The 10-gingerol Compound of Ginger in Inhibiting Cyclooxygenase-2 Activity Gabriella Chandrakirana Krisnamurti; Fatchiyah Fatchiyah
The Journal of Pure and Applied Chemistry Research Vol 9, No 3 (2020): Edition September-December 2020
Publisher : Chemistry Department, The University of Brawijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21776/ub.jpacr.2020.009.03.547

Abstract

Anti-inflammatory agents inhibit prostaglandin synthesis by blocking cyclooxygenases (COXs). The compounds extracted from ginger, 10-gingerol and 10-shogaol can inhibit inflammation but the mechanism of inhibition remains unclear. Here we used molecular docking to predict the molecular interactions between COXs and the three inhibitors, acetaminophen (CID1983), 10-gingerol (CID168115) and 10-shogaol (CID6442612). By using that acetaminophen as a gold standard, the results demonstrated that acetaminophen, 10-gingerol, and 10-shogaol could bind catalytic domain and membrane binding domain of cyclooxygenase-1 (COX-1) and cyclooxygenase-2 (COX-2). The 10-shogaol did not show significantly different binding energy to bind to COX-1 and COX-2. The 10-gingerol posed a stronger and more specific binding to the membrane-binding domain of COX-2 than acetaminophen and 10-shogaol. The specific binding of the 10-gingerol to COX-2 could prevent the binding of the natural substrate, arachidonic acid. The results provide useful information to improving activities of anti-inflammatory.
The Potential Role of Rosmarinic Acid and Sinensetin as α-Amylase Inhibitor: In Silico Study Hazna Noor Meidinna; Fatchiyah Fatchiyah
The Journal of Pure and Applied Chemistry Research Vol 8, No 1 (2019): Edition January-April 2019
Publisher : Chemistry Department, The University of Brawijaya

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.21776/ub.jpacr.2019.008.01.460

Abstract

The study of natural compound as α-amylase inhibitor has been a concern since the synthetic drugs for the management of type 2 diabetes mellitus have several side effects. The present study was carried out to predict the ability of rosmarinic acid and sinensetin as human α-amylase inhibitor by in silico study. All of the prepared 3D structures were used in the molecular docking by using Hex 8.0.0. The visualization of the molecular interactions of those compounds with human salivary α-amylase or human pancreatic α-amylase was established in the Discovery Studio Client 4.1 software. The result of this study determined that rosmarinic acid and sinensetin bound to the A domain of human pancreatic α-amylase and human salivary α-amylase. Rosmarinic acid-human salivary α-amylase complex was observed to possess high number of hydrogen bonds compared to sinensetin-human salivary α-amylase complex. The similar result was observed in the comparison of rosmarinic acid-human pancreatic α-amylase complex and sinensetin-human pancreatic α-amylase complex. The rosmarinic acid was able to bind the Glu233 of human pancreatic α-amylase. These data suggest rosmarinic acid as a potential inhibitor of human salivary α-amylase and human pancreatic α-amylase. Further experimental evidence is needed to confirm this observation.
Co-Authors Gabriella Chandrakirana Krisnamurti Hazna Noor Meidinna