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Journal : Science Midwifery

Anti-Inflammatory Test Macaranga gigantea with Interleukin Inhibitor approach In Silico samsul hadi; kunti nastiti
Science Midwifery Vol 10 No 5 (2022): December: Science Midwifery
Publisher : Institute of Computer Science (IOCS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35335/midwifery.v10i5.869

Abstract

Inflammation is condition inflammation accompanied by pain and fever . _ In general drug anti-inflammatory work with hinder enzyme cyclooxygenase , both COX-1 and COX-2, which play a role in synthesize inflammatory mediators such as prostaglandins and thromboxane . Various study developed for look for agent more therapy effective and have more risk low good symptom inflammation I or consequence period long from disease inflammation chronic . One of the approach taken is develop IL1β inhibitors. Method used is compound screening active using in silico. Docking software used in study this is autodock 4.2 and visualization interaction using discovery studio , materials used in study this is the compounds contained in M. gigantea. Result of research this is the value of delta G is negative below -4 kcal / mol, so reaction yanga occur between the ligand and the protein will walk spontaneous . Conclusion in study this obtained four ligands with lowest G value that is glycasperin A; broussoflavonol F; 5,7,3 ',4'-Tetrahydroxy-3-methoxy-8,5'-diprenylflavone; meliternatin .
Karamunting screening as an antifungal using the In Silico method targeting N-myristoyltransferase Samsul Hadi; Kunti Nastiti
Science Midwifery Vol 10 No 6 (2023): February: Midwifery and Health Sciences
Publisher : Institute of Computer Science (IOCS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35335/midwifery.v10i6.1134

Abstract

Karamunting has been empirically used by the community in overcoming itching disorders due to fungi. Therefore the purpose of this study was to screen in silico the content of Karamunting against N-myristoyltranseferase protein. The method used in this study was In Silico screening using PLANTS docking and the materials used were thirteen compounds contained in Karamunting. The results of this study are docking scores from -123.628 to -77.3801 and residues that have similarities with native ligands when interacting with N-myristoyltransferase, namely one to three amino acids, the predicted value using PASSonline ranges from 0.101 to 0.583. The conclusion of this study was obtained three compounds that have the potential as antifungals with the N-myristoyltransferase inhibitor mechanism, these compounds are α-tocopherol-quinone; α-tocopherol A; blumeatin.
Activity predication of rhodomyrtus tomentosa (Aiton) hassk against ace1 inhibitors Samsul Hadi; Kunti Nastiti
Science Midwifery Vol 11 No 2 (2023): June: Midwifery and Health Sciences
Publisher : Institute of Computer Science (IOCS)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.35335/midwifery.v11i2.1271

Abstract

ACE is a peptidyl-dipeptidase enzyme that catalyzes the conversion of substrates from angiotensin I to angiotensin II. These changes cause constriction of blood vessels so that blood pressure increases (hypertension), so This study aims to find compounds that have the potential to reduce blood pressure through the pathway of ACE1 enzyme inhibition. The method used is docking, the material used is a compound contained from Rhodomyrtus tomentosa and. The ACE1 protein was obtained from RCSB with the code 1UZF. The equipment used was an online pass webserver, PLNTS software and discovery studio. This research was started by redocking the native ligand to determine the coordinates and radius, followed by validating the docking results. The results of the early stage screening obtained 4 compounds with a threshold value above 0.3, these four compounds were continued with the docking test. The docking scores obtained were Afrormosin (-59.620); Pedunculagin (-45.205); Tomentosine (-70.986); Desgalloylstachyurin (-54.374). The conclusion obtained is that the Tomentosine compound binds most easily to ACE1