Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking

The present study used in vitro and in silico techniques, as well as the metabolomics approach to characterise α-glucosidase inhibitors from different fractions of Clinacanthus nutans. C. nutans is a medicinal plant belonging to the Acanthaceae family, and is traditionally used to treat diabetes in...

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Main Authors:	Murugesu, Suganya, Ibrahim, Zalikha, Ahmed, Qamar Uddin, Uzir, Bisha Fathamah, Nik Yusoff, Nik Mohd. Idris, Perumal, Vikneswari, Abas, Faridah, Shaari, Khozirah, Khatib, Alfi
Format:	Article
Language:	English English
Published:	Xi'an Jiaotong University 2019
Subjects:	Q Science (General)
Online Access:	http://irep.iium.edu.my/79140/ http://irep.iium.edu.my/79140/ http://irep.iium.edu.my/79140/ http://irep.iium.edu.my/79140/1/Murugesu%20et%20al%202019-JPA.pdf http://irep.iium.edu.my/79140/7/scopus_79140.pdf

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recordtype	eprints
spelling	iium-791402020-02-26T06:44:21Z http://irep.iium.edu.my/79140/ Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking Murugesu, Suganya Ibrahim, Zalikha Ahmed, Qamar Uddin Uzir, Bisha Fathamah Nik Yusoff, Nik Mohd. Idris Perumal, Vikneswari Abas, Faridah Shaari, Khozirah Khatib, Alfi Q Science (General) The present study used in vitro and in silico techniques, as well as the metabolomics approach to characterise α-glucosidase inhibitors from different fractions of Clinacanthus nutans. C. nutans is a medicinal plant belonging to the Acanthaceae family, and is traditionally used to treat diabetes in Malaysia. n-Hexane, n-hexane: ethyl acetate (1:1, v/v), ethyl acetate, ethyl acetate: methanol (1:1, v/v), and methanol fractions were obtained via partitioning of the 80% methanolic crude extract. The in vitro α-glucosidase inhibitory activity was analyzed using all the fractions collected, followed by profiling of the metabolites using liquid chromatography combined with mass spectrometry. The partial least square (PLS) statistical model was developed using the SIMCA P+14.0 software and the following four inhibitors were obtained: (1) 4,6,8-Megastigmatrien-3-one; (2) N-Isobutyl-2-nonen-6,8-diynamide; (3) 1′,2′-bis(acetyloxy)-3′,4′-didehydro-2′-hydro-β, ψ-carotene; and (4) 22-acetate-3-hydroxy-21-(6-methyl-2,4-octadienoate)-olean-12-en-28-oic acid. The in silico study performed via molecular docking with the crystal structure of yeast isomaltase (PDB code: 3A4A) involved a hydrogen bond and some hydrophobic interactions between the inhibitors and protein. The residues that interacted include ASN259, HID295, LYS156, ARG335, and GLY209 with a hydrogen bond, while TRP15, TYR158, VAL232, HIE280, ALA292, PRO312, LEU313, VAL313, PHE314, ARG315, TYR316, VAL319, and TRP343 with other forms of bonding. Xi'an Jiaotong University 2019-04-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/79140/1/Murugesu%20et%20al%202019-JPA.pdf application/pdf en http://irep.iium.edu.my/79140/7/scopus_79140.pdf Murugesu, Suganya and Ibrahim, Zalikha and Ahmed, Qamar Uddin and Uzir, Bisha Fathamah and Nik Yusoff, Nik Mohd. Idris and Perumal, Vikneswari and Abas, Faridah and Shaari, Khozirah and Khatib, Alfi (2019) Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking. Journal of Pharmaceutical Analysis, 9 (2). pp. 91-99. ISSN 20951779 https://www.sciencedirect.com/science/article/pii/S2095177918304659?via%3Dihub 10.1016/j.jpha.2018.11.001
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English
topic	Q Science (General)
spellingShingle	Q Science (General) Murugesu, Suganya Ibrahim, Zalikha Ahmed, Qamar Uddin Uzir, Bisha Fathamah Nik Yusoff, Nik Mohd. Idris Perumal, Vikneswari Abas, Faridah Shaari, Khozirah Khatib, Alfi Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
description	The present study used in vitro and in silico techniques, as well as the metabolomics approach to characterise α-glucosidase inhibitors from different fractions of Clinacanthus nutans. C. nutans is a medicinal plant belonging to the Acanthaceae family, and is traditionally used to treat diabetes in Malaysia. n-Hexane, n-hexane: ethyl acetate (1:1, v/v), ethyl acetate, ethyl acetate: methanol (1:1, v/v), and methanol fractions were obtained via partitioning of the 80% methanolic crude extract. The in vitro α-glucosidase inhibitory activity was analyzed using all the fractions collected, followed by profiling of the metabolites using liquid chromatography combined with mass spectrometry. The partial least square (PLS) statistical model was developed using the SIMCA P+14.0 software and the following four inhibitors were obtained: (1) 4,6,8-Megastigmatrien-3-one; (2) N-Isobutyl-2-nonen-6,8-diynamide; (3) 1′,2′-bis(acetyloxy)-3′,4′-didehydro-2′-hydro-β, ψ-carotene; and (4) 22-acetate-3-hydroxy-21-(6-methyl-2,4-octadienoate)-olean-12-en-28-oic acid. The in silico study performed via molecular docking with the crystal structure of yeast isomaltase (PDB code: 3A4A) involved a hydrogen bond and some hydrophobic interactions between the inhibitors and protein. The residues that interacted include ASN259, HID295, LYS156, ARG335, and GLY209 with a hydrogen bond, while TRP15, TYR158, VAL232, HIE280, ALA292, PRO312, LEU313, VAL313, PHE314, ARG315, TYR316, VAL319, and TRP343 with other forms of bonding.
format	Article
author	Murugesu, Suganya Ibrahim, Zalikha Ahmed, Qamar Uddin Uzir, Bisha Fathamah Nik Yusoff, Nik Mohd. Idris Perumal, Vikneswari Abas, Faridah Shaari, Khozirah Khatib, Alfi
author_facet	Murugesu, Suganya Ibrahim, Zalikha Ahmed, Qamar Uddin Uzir, Bisha Fathamah Nik Yusoff, Nik Mohd. Idris Perumal, Vikneswari Abas, Faridah Shaari, Khozirah Khatib, Alfi
author_sort	Murugesu, Suganya
title	Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
title_short	Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
title_full	Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
title_fullStr	Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
title_full_unstemmed	Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
title_sort	identiﬁcation of α-glucosidase inhibitors from clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking
publisher	Xi'an Jiaotong University
publishDate	2019
url	http://irep.iium.edu.my/79140/ http://irep.iium.edu.my/79140/ http://irep.iium.edu.my/79140/ http://irep.iium.edu.my/79140/1/Murugesu%20et%20al%202019-JPA.pdf http://irep.iium.edu.my/79140/7/scopus_79140.pdf
first_indexed	2023-09-18T21:51:17Z
last_indexed	2023-09-18T21:51:17Z
_version_	1777413786009862144

Identiﬁcation of α-glucosidase inhibitors from Clinacanthus nutans leaf extract using liquid chromatography-mass spectrometry-based metabolomics and protein-ligand interaction with molecular docking

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