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Molecular docking, synthesis and biological evaluation of ergosteryl-ferulate as a HMG-CoA reductase inhibitor
Aziz S.a,b, Elfahmia, Soemardji A.A.a, Sukrasnoa
a Pharmaceutical Biology Research Group, School of Pharmacy, Institut Teknologi Bandung, Indonesia
b Department of Pharmacy, Faculty of Science, Institut Teknologi Sumatera, Indonesia
[vc_row][vc_column][vc_row_inner][vc_column_inner][vc_separator css=”.vc_custom_1624529070653{padding-top: 30px !important;padding-bottom: 30px !important;}”][/vc_column_inner][/vc_row_inner][vc_row_inner layout=”boxed”][vc_column_inner width=”3/4″ css=”.vc_custom_1624695412187{border-right-width: 1px !important;border-right-color: #dddddd !important;border-right-style: solid !important;border-radius: 1px !important;}”][vc_empty_space][megatron_heading title=”Abstract” size=”size-sm” text_align=”text-left”][vc_column_text]© 2020 Pakistan Journal of Pharmaceutical Sciences. All rights reserved.In the present study, ergosteryl-ferulate (5), oryzanol analog was evaluated for its possibility as the inhibitor of HMG-CoA reductase (HMGR), through in silico and in vitro approach. Firstly, the study was conducted through molecular docking simulation using AutoDock Tools software to predict the interaction of 5 in complexes with HMGR. In addition, four major compounds of oryzanol (1-4) were employed as a comparison. Secondly, 5 was synthesized through esterification using thionyl chloride as an activator. Lastly, 5 was evaluated for its capacity to inhibit HMGR activity using HMGR assay kit. Molecular docking simulation results suggest that oryzanol (1-4) and 5 exhibited a binding affinity against HMGR. The activity of 5 was predicted to be the best among the oryzanol compounds (1-4), in which, the free binding energy and inhibition constant were -4.17 kcal/mol and 0.88mM. The in vitro assay showed that 5 had inhibitory activity against HMGR 1.93 times higher than oryzanol. In summary, 5 has more potential candidates for HMGR inhibitor than oryzanol.[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Author keywords” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Indexed keywords” size=”size-sm” text_align=”text-left”][vc_column_text]Docking,Ergosteryl-ferulate,Esterification,HMG-CoA reductase,Oryzanol[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Funding details” size=”size-sm” text_align=”text-left”][vc_column_text]This research was funded by Institut Teknologi Bandung research grant, with contract number 007/I1.Bo4/PL/2017.[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”DOI” size=”size-sm” text_align=”text-left”][vc_column_text]https://doi.org/10.36721/PJPS.2020.33.3.REG.997-1003.1[/vc_column_text][/vc_column_inner][vc_column_inner width=”1/4″][vc_column_text]Widget Plumx[/vc_column_text][/vc_column_inner][/vc_row_inner][/vc_column][/vc_row][vc_row][vc_column][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][/vc_column][/vc_row]