TY  - JOUR 
AU  - Abdjan, Muhammad Ikhlas 
AU  - Aminah, Nanik Siti 
AU  - Kristanti, Alfinda Novi 
AU  - Siswanto, Imam 
AU  - Windah, Axl Laurens Lukas 
AU  - Thant, Tin Myo 
AU  - Ramadhan, Rico 
AU  - Takaya, Yoshiaki 
AU  - Ul-Haq, Zaheer Ul 
AU  - Choudhary, Muhammad Iqbal 
PY  - 2024 
T1  - Computational Studies on Carbazole-Pyranocoumarin Conjugate Against α-glucosidase Enzyme 
JO  - Engineered Science 
SP  - 1286 
EP  -  
VL  - 31 
AB  - α-Glucosidase is an enzyme responsible for releasing the α-D-glucose monomer through hydrolysis reactions. The release of this monomer increases the sugar concentration in the blood and increases the risk of type-2 diabetes mellitus (DM) patients. Through computational studies, we evaluate the structural and inhibitory efficiency of the new carbazole-pyranocoumarin conjugate/Carbazomarin-C as α-Glucosidase inhibitor at the molecular level. We found that Carbazomarin-C (Car) has promising drug-likeness and ADMET properties. Meanwhile, proton chemical shift modeling through a density functional theory (DFT) approach shows that the Car molecule had an agreement with experimental results. Molecular dynamics simulation was applied to understand their inhibitory efficiency through free energy binding (∆Gbind and ∆Gexp). The results showed that Car (∆Gbind: -6.10 kcal/mol and ∆Gexp: -5.02 kcal/mol) had better inhibition than Acarbose as a control (∆Gbind: -4.48 kcal/mol and ∆Gexp: -3.17 kcal/mol). Moreover, nine residues were responsible for the bond stabilization of both inhibitors, namely F175, R210, V213, Q276, F300, P309, L310, R439, and R443. The information in this work demonstrated how potential Carbazomarin-C is as an α-Glucosidase inhibitor at the molecular level.SN  - 2576-9898 
UR  - http://dx.doi.org/10.30919/es1286 
DO  - 10.30919/es1286 
ID  - es1286