In silico study of the ErbB4 interactions with curcumin analogs

Curcumin (diferuloylmethane) is generally found as the major compound in rhizomes of turmeric plants Curcuma longa Linaeusas. Curcumin has been shown to inhibit cancer growth by means of inhibiting ErBB family members (ErbB1, Erbb2, ErbB3 and ErbB4). This family receptors often targeted for developm...

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Main Authors:	Azman, Putri Arsyadian, Abd Halim, Khairul Bariyyah
Format:	Conference or Workshop Item
Language:	English
Published:	2015
Subjects:	R Medicine (General)
Online Access:	http://irep.iium.edu.my/48249/ http://irep.iium.edu.my/48249/ http://irep.iium.edu.my/48249/1/48249.pdf

id	iium-48249
recordtype	eprints
spelling	iium-482492016-04-28T03:18:06Z http://irep.iium.edu.my/48249/ In silico study of the ErbB4 interactions with curcumin analogs Azman, Putri Arsyadian Abd Halim, Khairul Bariyyah R Medicine (General) Curcumin (diferuloylmethane) is generally found as the major compound in rhizomes of turmeric plants Curcuma longa Linaeusas. Curcumin has been shown to inhibit cancer growth by means of inhibiting ErBB family members (ErbB1, Erbb2, ErbB3 and ErbB4). This family receptors often targeted for development of cancer therapeutics. Previously, curcumin has also been shown to selectively inhibit EGFR or ErbB1 in in vitro, in vivo as well as in silico studies. However, its inhibitive effect on ErbB4 has not been elucidated. The present study evaluated the efficacy of natural curcumin and its analogs as ErbB4 inhibitors using computational approach namely molecular docking and molecular dynamics simulation. These approaches have been used to investigate the interactions between ErbB4 with curcumin analogs. Our molecular docking simulation showed that among five ligands that were docked at the active site cavity of ErbB4, ligand D docked with the lowest binding energy which was -7.29 kcal/mol. Ligand D which was the lowest energy complex obtained from docking experiment was then further investigated using molecular dynamics simulations. Ligand D were quite well oriented in the binding pocket throughout the 10 ns simulations. Molecular docking and molecular dynamics (MD) simulation studies showed that curcumin could be embedded into the hydrophobic pocket of ErbB4 and form stable hydrogen bonding interactions mainly with residue LYS-59. In conclusion, we have explored the binding mechanism of curcumin binding to ErbB4. This work could offer useful insight for designing novel analogs of curcumin as potential ErbB family inhibitors in the future. 2015 Conference or Workshop Item NonPeerReviewed application/pdf en http://irep.iium.edu.my/48249/1/48249.pdf Azman, Putri Arsyadian and Abd Halim, Khairul Bariyyah (2015) In silico study of the ErbB4 interactions with curcumin analogs. In: 6th Regional Conference on Molecular Medicine (RCMM) in Conjunction with 2nd National Conference for Cancer Research 2015, 23rd-25th Oct. 2015, Sunway Putra Hotel, Kuala Lumpur. (Unpublished) http://www.ukm.my/umbi/wp-content/uploads/RCMM_ABSTRACT_BOOK_2015_final.pdf
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	R Medicine (General)
spellingShingle	R Medicine (General) Azman, Putri Arsyadian Abd Halim, Khairul Bariyyah In silico study of the ErbB4 interactions with curcumin analogs
description	Curcumin (diferuloylmethane) is generally found as the major compound in rhizomes of turmeric plants Curcuma longa Linaeusas. Curcumin has been shown to inhibit cancer growth by means of inhibiting ErBB family members (ErbB1, Erbb2, ErbB3 and ErbB4). This family receptors often targeted for development of cancer therapeutics. Previously, curcumin has also been shown to selectively inhibit EGFR or ErbB1 in in vitro, in vivo as well as in silico studies. However, its inhibitive effect on ErbB4 has not been elucidated. The present study evaluated the efficacy of natural curcumin and its analogs as ErbB4 inhibitors using computational approach namely molecular docking and molecular dynamics simulation. These approaches have been used to investigate the interactions between ErbB4 with curcumin analogs. Our molecular docking simulation showed that among five ligands that were docked at the active site cavity of ErbB4, ligand D docked with the lowest binding energy which was -7.29 kcal/mol. Ligand D which was the lowest energy complex obtained from docking experiment was then further investigated using molecular dynamics simulations. Ligand D were quite well oriented in the binding pocket throughout the 10 ns simulations. Molecular docking and molecular dynamics (MD) simulation studies showed that curcumin could be embedded into the hydrophobic pocket of ErbB4 and form stable hydrogen bonding interactions mainly with residue LYS-59. In conclusion, we have explored the binding mechanism of curcumin binding to ErbB4. This work could offer useful insight for designing novel analogs of curcumin as potential ErbB family inhibitors in the future.
format	Conference or Workshop Item
author	Azman, Putri Arsyadian Abd Halim, Khairul Bariyyah
author_facet	Azman, Putri Arsyadian Abd Halim, Khairul Bariyyah
author_sort	Azman, Putri Arsyadian
title	In silico study of the ErbB4 interactions with curcumin analogs
title_short	In silico study of the ErbB4 interactions with curcumin analogs
title_full	In silico study of the ErbB4 interactions with curcumin analogs
title_fullStr	In silico study of the ErbB4 interactions with curcumin analogs
title_full_unstemmed	In silico study of the ErbB4 interactions with curcumin analogs
title_sort	in silico study of the erbb4 interactions with curcumin analogs
publishDate	2015
url	http://irep.iium.edu.my/48249/ http://irep.iium.edu.my/48249/ http://irep.iium.edu.my/48249/1/48249.pdf
first_indexed	2023-09-18T21:08:29Z
last_indexed	2023-09-18T21:08:29Z
_version_	1777411093146107904

In silico study of the ErbB4 interactions with curcumin analogs

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