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All Journal ad-Dawaa : Journal of Pharmaceutical Sciences Indonesian Journal of Pharmacy and Natural Product
Wismayani, Leni
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Biochemistry, Genetics & Molecular Biology Chemistry Immunology & microbiology Materials Science & Nanotechnology Medicine & Pharmacology

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Journal : ad-Dawaa : Journal of Pharmaceutical Sciences

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HMG-CoA Reductase Inhibitory Activity Potential of Iota-, Kappa-, and Lambda-carrageenan: A Molecular Docking Approach Setiawansyah, Arif; Muh Ikhlas Arsul; Adliani, Nur; Wismayani, Leni
Ad-Dawaa: Journal of Pharmaceutical Sciences Vol 5 No 2 (2022)
Publisher : Universitas Islam Negeri Alauddin Makassar

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24252/djps.v5i2.32721

Abstract

HMG-CoA reductase is an essential enzyme responsible for the biosynthesis of cholesterol. Hyperactivity of HMG-CoA reductase will increase cholesterol production, leading to the elevation of blood cholesterol levels. Inhibition of HMG-CoA reductase is one way to block cholesterol biosynthesis to lower blood cholesterol levels. This study evaluated the inhibitory potential of iota-, kappa-, and lambda-carrageenan against HMG-CoA reductase. The study was undertaken by in silico method using a molecular docking approach via Autodock 4.2 assisted by ADT graphical user interface. HMG-CoA reductase co-crystal structure was used as the target, and iota-, kappa-, and lambda-carrageenan as the test ligands. The result revealed that iota- and lambda-carrageenan possess an excellent affinity to HMG-CoA reductase with the free binding energy of -12.44 and -11.87 kcal/mol and Ki value of 0.765 and 2.01 nM, respectively, which is found to be better than Simvastatin and the native ligand. The compounds' chemical properties influenced the molecules' molecular interactions affecting their affinity. The number of SO4 groups is assumed to affect the HMG-CoA reductase inhibitory activity of iota-, kappa-, and lambda-carrageenan. KEYWORDS: iota-, kappa-, and lambda-carrageenan; HMG-CoA reductase; inhibitory activity; molecular docking
Aaptamine Enhanced Doxorubicin Activity on B-Cell Lymphoma 2 (Bcl-2): A Multi-Structural Molecular Docking Study Setiawansyah, Arif; Susanti, Gita; Alrayan, Reza; Hadi, Ismanurrahman; Ikhlas Arsul, Muhammad; Luthfiana, Dewi; Wismayani, Leni; Hidayati, Nurul
Ad-Dawaa: Journal of Pharmaceutical Sciences Vol. 7 No. 1 (2024)
Publisher : Universitas Islam Negeri Alauddin Makassar

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24252/djps.v7i1.46796

Abstract

Doxorubicin, a widely used chemotherapeutic agent, targets Bcl-2, but its efficacy can be limited by drug resistance. Its combination with natural derived compound can be a therapeutic approach to overcome this problem. This study aimed to investigate the molecular interactions and binding affinities of aaptamine and doxorubicin with Bcl-2 using molecular docking simulations, and to evaluate the potential synergistic effects of their combination. Molecular docking studies were performed to predict the binding modes and affinities of aaptamine and doxorubicin along with their combination to Bcl-2. Molecular docking simulation results showed that aaptamine binds to the BH3 binding groove of Bcl-2, forming key interactions with residues like Asp70, Tyr67, Phe112 and Glu111. Aaptamine stabilized the binding of doxorubicin to Bcl-2 through hydrophobic bonding and van der Waals interactions, resulting in enhanced binding affinity. The combination of aaptamine and doxorubicin exhibits synergistic anticancer effects by enhancing the binding affinity of doxorubicin to Bcl-2. Molecular docking simulations provided insights into the stabilizing interactions between aaptamine, doxorubicin, and Bcl-2, suggesting a potential strategy for overcoming Bcl-2-mediated drug resistance in cancer. However, further in vitro investigation is needed to be implemented.
Co-Authors Alrayan, Reza Arif Setiawansyah Gita Susanti, Gita Hadi, Ismanurrahman Ikhlas Arsul, Muhammad Luthfiana, Dewi Muh Ikhlas Arsul Nur Adliani Nurul Hidayati Roni, Abdul Tri Minarsih