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Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches

Neoculin is a sweet taste protein capable of modifying sour taste into sweet taste. Neoculin, along with other sweeteners, are received by the human sweet taste receptors T1R2 and T1R3. To date, there has been few studies regarding how neoculin interacts with the human sweet taste receptors in molec...

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Main Authors: Yousif, Ragheed Hussam, A. Wahab, Habibah, Shameli, Kamyar, Ahmad Khairudin, Nurul Bahiyah
Format: Article
Language:English
Published: Penerbit Universiti Kebangsaan Malaysia 2020
Subjects:
T Technology (General)
Online Access:http://eprints.utm.my/id/eprint/93942/1/NurulbahiyahAhmadKhairudin2020_ExploringtheMolecularInteractionsbetweenNeoculinandtheHuman.pdf
http://eprints.utm.my/id/eprint/93942/
http://dx.doi.org/10.17576/jsm-2020-4903-06
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spelling my.utm.939422022-02-28T13:18:39Z http://eprints.utm.my/id/eprint/93942/ Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches Yousif, Ragheed Hussam A. Wahab, Habibah Shameli, Kamyar Ahmad Khairudin, Nurul Bahiyah T Technology (General) Neoculin is a sweet taste protein capable of modifying sour taste into sweet taste. Neoculin, along with other sweeteners, are received by the human sweet taste receptors T1R2 and T1R3. To date, there has been few studies regarding how neoculin interacts with the human sweet taste receptors in molecular level. In this study, computational approaches were applied to elucidate how neoculin interact with T1R2 and T1R3 at molecular level. In order to achieve this research, homology modeling for T1R2 and T1R3 was performed to predict their structure. A protein-protein docking study was conducted between neoculin and T1R2 and T1R3, which displayed a strong relationship with the previous experimental findings regarding the important residues of neoculin, and how they interact with the ATD domain of T1R3. These residues are His11, Asp91, Tyr21, Asn44, Arg48, Tyr 65, Val72, and Phe94. The best docked complexes were then subjected to molecular dynamics simulation for further analysis. The molecular dynamics simulation results showed the contributions of the important residues of neoculin in forming hydrogen bonds with the residues of the receptors. The binding energy between neoculin and each of T1R2 and T1R3 were also calculated. These results concluded that neoculin sweet taste and taste modifying abilities are only active when it binds to the amino terminal domain of T1R3. Penerbit Universiti Kebangsaan Malaysia 2020 Article PeerReviewed application/pdf en http://eprints.utm.my/id/eprint/93942/1/NurulbahiyahAhmadKhairudin2020_ExploringtheMolecularInteractionsbetweenNeoculinandtheHuman.pdf Yousif, Ragheed Hussam and A. Wahab, Habibah and Shameli, Kamyar and Ahmad Khairudin, Nurul Bahiyah (2020) Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches. Sains Malaysiana, 49 (3). pp. 517-525. ISSN 0126-6039 http://dx.doi.org/10.17576/jsm-2020-4903-06
institution Universiti Teknologi Malaysia
building UTM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Teknologi Malaysia
content_source UTM Institutional Repository
url_provider http://eprints.utm.my/
language English
topic T Technology (General)
spellingShingle T Technology (General)
Yousif, Ragheed Hussam
A. Wahab, Habibah
Shameli, Kamyar
Ahmad Khairudin, Nurul Bahiyah
Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
description Neoculin is a sweet taste protein capable of modifying sour taste into sweet taste. Neoculin, along with other sweeteners, are received by the human sweet taste receptors T1R2 and T1R3. To date, there has been few studies regarding how neoculin interacts with the human sweet taste receptors in molecular level. In this study, computational approaches were applied to elucidate how neoculin interact with T1R2 and T1R3 at molecular level. In order to achieve this research, homology modeling for T1R2 and T1R3 was performed to predict their structure. A protein-protein docking study was conducted between neoculin and T1R2 and T1R3, which displayed a strong relationship with the previous experimental findings regarding the important residues of neoculin, and how they interact with the ATD domain of T1R3. These residues are His11, Asp91, Tyr21, Asn44, Arg48, Tyr 65, Val72, and Phe94. The best docked complexes were then subjected to molecular dynamics simulation for further analysis. The molecular dynamics simulation results showed the contributions of the important residues of neoculin in forming hydrogen bonds with the residues of the receptors. The binding energy between neoculin and each of T1R2 and T1R3 were also calculated. These results concluded that neoculin sweet taste and taste modifying abilities are only active when it binds to the amino terminal domain of T1R3.
format Article
author Yousif, Ragheed Hussam
A. Wahab, Habibah
Shameli, Kamyar
Ahmad Khairudin, Nurul Bahiyah
author_facet Yousif, Ragheed Hussam
A. Wahab, Habibah
Shameli, Kamyar
Ahmad Khairudin, Nurul Bahiyah
author_sort Yousif, Ragheed Hussam
title Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
title_short Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
title_full Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
title_fullStr Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
title_full_unstemmed Exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
title_sort exploring the molecular interactions between neoculin and the human sweet taste receptors through computational approaches
publisher Penerbit Universiti Kebangsaan Malaysia
publishDate 2020
url http://eprints.utm.my/id/eprint/93942/1/NurulbahiyahAhmadKhairudin2020_ExploringtheMolecularInteractionsbetweenNeoculinandtheHuman.pdf
http://eprints.utm.my/id/eprint/93942/
http://dx.doi.org/10.17576/jsm-2020-4903-06
_version_ 1726791457314963456
score 13.211869

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