In silico study of carvone derivatives as potential neuraminidase inhibitors

Recent outbreaks of highly pathogenic influenza strains have highlighted the need to develop new anti-influenza drugs. Here, we report an in silico study of carvone derivatives to analyze their binding modes with neuraminidase (NA) active sites. Two proposed carvone analogues, CV(A) and CV(B), with...

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Main Authors:	Jusoh, Noorakmar, Zainal, Hasanuddin, Abdul Hamid, Azzmer Azzar, Muhamad Bunnori, Noraslinda, Abd Halim, Khairul Bariyyah, Abd Hamid, Shafida
Format:	Article
Language:	English English English
Published:	Springer Berlin Heidelberg 2018
Subjects:	Q Science (General) QD Chemistry
Online Access:	http://irep.iium.edu.my/63210/ http://irep.iium.edu.my/63210/ http://irep.iium.edu.my/63210/ http://irep.iium.edu.my/63210/7/63210%20In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors%20SCOPUS.pdf http://irep.iium.edu.my/63210/13/63210_In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors_article.pdf http://irep.iium.edu.my/63210/19/63210_In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors_WoS.pdf

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recordtype	eprints
spelling	iium-632102018-10-19T01:26:36Z http://irep.iium.edu.my/63210/ In silico study of carvone derivatives as potential neuraminidase inhibitors Jusoh, Noorakmar Zainal, Hasanuddin Abdul Hamid, Azzmer Azzar Muhamad Bunnori, Noraslinda Abd Halim, Khairul Bariyyah Abd Hamid, Shafida Q Science (General) QD Chemistry Recent outbreaks of highly pathogenic influenza strains have highlighted the need to develop new anti-influenza drugs. Here, we report an in silico study of carvone derivatives to analyze their binding modes with neuraminidase (NA) active sites. Two proposed carvone analogues, CV(A) and CV(B), with 36 designed ligands were predicted to inhibit NA (PDB ID: 3TI6) using molecular docking. The design is based on structural resemblance with the commercial inhibitor, oseltamivir (OTV), ligand polarity, and amino acid residues in the NA active sites. Docking simulations revealed that ligand A18 has the lowest energy binding (ΔGbind) value of −8.30 kcal mol-1, comparable to OTV with ΔGbind of −8.72 kcal mol-1. A18 formed seven hydrogen bonds (H-bonds) at residues Arg292, Arg371, Asp151, Trp178, Glu227, and Tyr406, while eight H-bonds were formed by OTV with amino acids Arg118, Arg292, Arg371, Glu119, Asp151, and Arg152. Molecular dynamics (MD) simulation was conducted to compare the stability between ligand A18 and OTV with NA. Our simulation study showed that the A18-NA complex is as stable as the OTV-NA complex during the MD simulation of 50 ns through the analysis of RMSD, RMSF, total energy, hydrogen bonding, and MM/PBSA free energy calculations. Springer Berlin Heidelberg 2018-04-01 Article PeerReviewed application/pdf en http://irep.iium.edu.my/63210/7/63210%20In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors%20SCOPUS.pdf application/pdf en http://irep.iium.edu.my/63210/13/63210_In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors_article.pdf application/pdf en http://irep.iium.edu.my/63210/19/63210_In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors_WoS.pdf Jusoh, Noorakmar and Zainal, Hasanuddin and Abdul Hamid, Azzmer Azzar and Muhamad Bunnori, Noraslinda and Abd Halim, Khairul Bariyyah and Abd Hamid, Shafida (2018) In silico study of carvone derivatives as potential neuraminidase inhibitors. Journal of Molecular Modeling, 24 (4). pp. 1-13. ISSN 1610-2940 E-ISSN 0948-5023 https://link.springer.com/article/10.1007/s00894-018-3619-6 10.1007/s00894-018-3619-6
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English English English
topic	Q Science (General) QD Chemistry
spellingShingle	Q Science (General) QD Chemistry Jusoh, Noorakmar Zainal, Hasanuddin Abdul Hamid, Azzmer Azzar Muhamad Bunnori, Noraslinda Abd Halim, Khairul Bariyyah Abd Hamid, Shafida In silico study of carvone derivatives as potential neuraminidase inhibitors
description	Recent outbreaks of highly pathogenic influenza strains have highlighted the need to develop new anti-influenza drugs. Here, we report an in silico study of carvone derivatives to analyze their binding modes with neuraminidase (NA) active sites. Two proposed carvone analogues, CV(A) and CV(B), with 36 designed ligands were predicted to inhibit NA (PDB ID: 3TI6) using molecular docking. The design is based on structural resemblance with the commercial inhibitor, oseltamivir (OTV), ligand polarity, and amino acid residues in the NA active sites. Docking simulations revealed that ligand A18 has the lowest energy binding (ΔGbind) value of −8.30 kcal mol-1, comparable to OTV with ΔGbind of −8.72 kcal mol-1. A18 formed seven hydrogen bonds (H-bonds) at residues Arg292, Arg371, Asp151, Trp178, Glu227, and Tyr406, while eight H-bonds were formed by OTV with amino acids Arg118, Arg292, Arg371, Glu119, Asp151, and Arg152. Molecular dynamics (MD) simulation was conducted to compare the stability between ligand A18 and OTV with NA. Our simulation study showed that the A18-NA complex is as stable as the OTV-NA complex during the MD simulation of 50 ns through the analysis of RMSD, RMSF, total energy, hydrogen bonding, and MM/PBSA free energy calculations.
format	Article
author	Jusoh, Noorakmar Zainal, Hasanuddin Abdul Hamid, Azzmer Azzar Muhamad Bunnori, Noraslinda Abd Halim, Khairul Bariyyah Abd Hamid, Shafida
author_facet	Jusoh, Noorakmar Zainal, Hasanuddin Abdul Hamid, Azzmer Azzar Muhamad Bunnori, Noraslinda Abd Halim, Khairul Bariyyah Abd Hamid, Shafida
author_sort	Jusoh, Noorakmar
title	In silico study of carvone derivatives as potential neuraminidase inhibitors
title_short	In silico study of carvone derivatives as potential neuraminidase inhibitors
title_full	In silico study of carvone derivatives as potential neuraminidase inhibitors
title_fullStr	In silico study of carvone derivatives as potential neuraminidase inhibitors
title_full_unstemmed	In silico study of carvone derivatives as potential neuraminidase inhibitors
title_sort	in silico study of carvone derivatives as potential neuraminidase inhibitors
publisher	Springer Berlin Heidelberg
publishDate	2018
url	http://irep.iium.edu.my/63210/ http://irep.iium.edu.my/63210/ http://irep.iium.edu.my/63210/ http://irep.iium.edu.my/63210/7/63210%20In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors%20SCOPUS.pdf http://irep.iium.edu.my/63210/13/63210_In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors_article.pdf http://irep.iium.edu.my/63210/19/63210_In%20silico%20study%20of%20carvone%20derivatives%20as%20potential%20neuraminidase%20inhibitors_WoS.pdf
first_indexed	2023-09-18T21:29:39Z
last_indexed	2023-09-18T21:29:39Z
_version_	1777412425563242496

In silico study of carvone derivatives as potential neuraminidase inhibitors

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