Evidence map›Paper›PMID 39020086›Full record

ArticleCell biochemistry and biophysics2024

In Silico Exploration of Isoxazole Derivatives of Usnic Acid: Novel Therapeutic Prospects Against α-Amylase for Diabetes Treatment.

Miah Roney, Abdul Rashid Issahaku, A K M Moyeenul Huq, Suhaila Sapari, Fazira Ilyana Abdul Razak, Anke Wilhelm, Normaiza Binti Zamri, Sabrina Sharmin, Md Rabiul Islam, Mohd Fadhlizil Fasihi Mohd Aluwi

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Article in Cell biochemistry and biophysics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Miah RoneyFaculty of Industrial Sciences and Technology, Universiti Malaysia Pahang Al-Sultan Abdullah, Lebuhraya Persiaran Tun Khalil Yaakob, Kuantan, Pahang, Malaysia.
Abdul Rashid IssahakuDepartment of Chemistry, University of the Free State, 205 Nelson Mandela Avenue, Bloemfontein, 9301, South Africa.
A K M Moyeenul HuqCentre for Drug and Herbal Development, Faculty of Pharmacy, Universiti Kebangsaan Malaysia, Jalan Raja Muda Abdul Aziz-50300, Kuala Lumpur, Malaysia.
Suhaila SapariDepartment of Chemistry, Faculty of Science, University Technology of Malaysia, Skudai, 81310, Johor Bahru, Johor, Malaysia.
Fazira Ilyana Abdul RazakDepartment of Chemistry, Faculty of Science, University Technology of Malaysia, Skudai, 81310, Johor Bahru, Johor, Malaysia.
Anke WilhelmDepartment of Chemistry, University of the Free State, 205 Nelson Mandela Avenue, Bloemfontein, 9301, South Africa.
Normaiza Binti ZamriFaculty of Industrial Sciences and Technology, Universiti Malaysia Pahang Al-Sultan Abdullah, Lebuhraya Persiaran Tun Khalil Yaakob, Kuantan, Pahang, Malaysia.
Sabrina SharminSchool of Pharmacy, BRAC University, 66 Mohakhali, Dhaka, 1212, Bangladesh.
Md Rabiul IslamSchool of Pharmacy, BRAC University, 66 Mohakhali, Dhaka, 1212, Bangladesh.
Mohd Fadhlizil Fasihi Mohd AluwiFaculty of Industrial Sciences and Technology, Universiti Malaysia Pahang Al-Sultan Abdullah, Lebuhraya Persiaran Tun Khalil Yaakob, Kuantan, Pahang, Malaysia. fasihi@umpsa.edu.my.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diabetes mellitus (DM) a metabolic disorder characterized by high blood sugar levels causing damage to various organs over time. Current anti-diabetic drugs have limitations and side effects, prompting a search for new inhibitors targeting the α-amylase enzyme. This study aims to discover such inhibitors from thirty isoxazole derivatives of usnic acid using in silico approaches. The potential inhibitory effects of compounds were investigated using ADMET, molecular docking, molecular dynamic simulation, principal component analysis and density functional theory studies. ADMET analysis exhibited a wide range of physicochemical, pharmacokinetic, and drug-like qualities with no significant side effects which were then investigated using molecular docking experiment to determine the lead compound with the best binding affinity for the α-amylase enzyme. All compounds showed good binding affinity against α-amylase enzyme (-7.9 to -9.2 kcal/mol) where compound-13 showed the best binding affinity of -9.2 kcal/mol forming hydrogen bonds with Leu162, Tyr62, Glu233 and Asp300 amino acids. Furthermore, the binding posture and the stability of the compound-13-α-amylase enzyme complex was confirmed by molecular dynamic simulation experiment. Moreover, compound-13 showed binding energy value of -27.92 ± 5.61 kcal/mol, which indicated it could be an α-amylase inhibitor. Additionally, the reactivity of compound-13 was further confirmed by density functional theory analysis. The above findings suggest compound-13 to be a potential α-amylase inhibitor in DM. And setting the stage for further in vitro and in vivo experimental validation.

Indexed as

alpha-AmylasesBenzofuransHydrogen BondingIsoxazolesMolecular Docking SimulationMolecular Dynamics SimulationBinding SitesCatalytic DomainComputer SimulationDiabetes MellitusEnzyme InhibitorsHumansHypoglycemic AgentsPrincipal Component AnalysisProtein BindingThermodynamicsalpha-AmylasesBenzofuransEnzyme InhibitorsHypoglycemic AgentsIsoxazolesusnic acidAnti-diabeticDFTdockingMD Simulationα-amylase

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.