Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation

The ability of surfactant-like peptides to emulsify oil has become the main focus of our current study. We predicted the ability of a series of surfactant-like peptides (G6D, A6D, M6D, F6D, L6D, V6D, and I6D) to emulsify decane molecules using coarse-grained molecular dynamics simulations. A 1-μs si...

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Autores principales:	Tegar Wijaya, Rukman Hertadi
Formato:	article
Lenguaje:	EN
Publicado:	Department of Chemistry, Universitas Gadjah Mada 2019
Materias:	coarse-grained molecular dynamic simulation emulsion MARTINI peptide surfactant Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/7985ced411194ac08165f24f9fe92f33
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spelling	oai:doaj.org-article:7985ced411194ac08165f24f9fe92f332021-12-02T13:22:14ZEstimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation1411-94202460-157810.22146/ijc.34547https://doaj.org/article/7985ced411194ac08165f24f9fe92f332019-05-01T00:00:00Zhttps://jurnal.ugm.ac.id/ijc/article/view/34547https://doaj.org/toc/1411-9420https://doaj.org/toc/2460-1578The ability of surfactant-like peptides to emulsify oil has become the main focus of our current study. We predicted the ability of a series of surfactant-like peptides (G6D, A6D, M6D, F6D, L6D, V6D, and I6D) to emulsify decane molecules using coarse-grained molecular dynamics simulations. A 1-μs simulation of each peptide was carried out at 298 K and 1 atm using MARTINI force field. Simulation system was constructed to consist of 100 peptide molecules, 20 decane molecules, water, antifreeze particles and neutralizing ions in a random configuration. Out of seven tested peptides, M6D, F6D, L6D, V6D, and I6D were able to form emulsion while G6D and A6D self-assembled to order b-strands. A higher hydropathy index of amino acids constituting the hydrophobic tail renders the formation of an emulsion by peptides more likely. By calculating contact number between peptides and decanes, we found that emulsion stability and geometry depends on the structure of amino acids constituting the hydrophobic tail. Analysis of simulation trajectory revealed that emulsions are formed by small nucleation following by fusion to form a bigger emulsion. This study reveals the underlying principle at the molecular level of surfactant peptide ability to form an emulsion with hydrophobic molecules.Tegar WijayaRukman HertadiDepartment of Chemistry, Universitas Gadjah Madaarticlecoarse-grained molecular dynamic simulationemulsionMARTINIpeptidesurfactantChemistryQD1-999ENIndonesian Journal of Chemistry, Vol 19, Iss 3, Pp 599-605 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	coarse-grained molecular dynamic simulation emulsion MARTINI peptide surfactant Chemistry QD1-999
spellingShingle	coarse-grained molecular dynamic simulation emulsion MARTINI peptide surfactant Chemistry QD1-999 Tegar Wijaya Rukman Hertadi Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation
description	The ability of surfactant-like peptides to emulsify oil has become the main focus of our current study. We predicted the ability of a series of surfactant-like peptides (G6D, A6D, M6D, F6D, L6D, V6D, and I6D) to emulsify decane molecules using coarse-grained molecular dynamics simulations. A 1-μs simulation of each peptide was carried out at 298 K and 1 atm using MARTINI force field. Simulation system was constructed to consist of 100 peptide molecules, 20 decane molecules, water, antifreeze particles and neutralizing ions in a random configuration. Out of seven tested peptides, M6D, F6D, L6D, V6D, and I6D were able to form emulsion while G6D and A6D self-assembled to order b-strands. A higher hydropathy index of amino acids constituting the hydrophobic tail renders the formation of an emulsion by peptides more likely. By calculating contact number between peptides and decanes, we found that emulsion stability and geometry depends on the structure of amino acids constituting the hydrophobic tail. Analysis of simulation trajectory revealed that emulsions are formed by small nucleation following by fusion to form a bigger emulsion. This study reveals the underlying principle at the molecular level of surfactant peptide ability to form an emulsion with hydrophobic molecules.
format	article
author	Tegar Wijaya Rukman Hertadi
author_facet	Tegar Wijaya Rukman Hertadi
author_sort	Tegar Wijaya
title	Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation
title_short	Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation
title_full	Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation
title_fullStr	Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation
title_full_unstemmed	Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation
title_sort	estimating factors determining emulsification capability of surfactant-like peptide with coarse-grained molecular dynamics simulation
publisher	Department of Chemistry, Universitas Gadjah Mada
publishDate	2019
url	https://doaj.org/article/7985ced411194ac08165f24f9fe92f33
work_keys_str_mv	AT tegarwijaya estimatingfactorsdeterminingemulsificationcapabilityofsurfactantlikepeptidewithcoarsegrainedmoleculardynamicssimulation AT rukmanhertadi estimatingfactorsdeterminingemulsificationcapabilityofsurfactantlikepeptidewithcoarsegrainedmoleculardynamicssimulation
_version_	1718393159714603008

Estimating Factors Determining Emulsification Capability of Surfactant-Like Peptide with Coarse-Grained Molecular Dynamics Simulation

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