Journal
JOURNAL OF MOLECULAR LIQUIDS
Volume 341, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.molliq.2021.117261
Keywords
Molecular Dynamics; Amino acids; Peptide; Laminar structure; HB dynamics
Funding
- CNPq - Conselho Nacional de Desenvolvimento Cientifico e Tecnologico, Brazil [304903/2020-5]
- CAPES - Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior
- FAPEG - Fundacao de Amparo a Pesquisa do Estado de Goias [201810267000740]
- IFG - Instituto Federal de Goias
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In this study, we used classical molecular dynamics simulations to evaluate laminar structures formed by peptides with the (RF)(5) primary sequence. Our theoretical results indicate that these structures more closely resemble a laminar form, rather than membrane-like or fiber-like nanostructures. The dense mesh of hydrogen bonds in the nanostructures allows for the separation of hydrophilic and hydrophobic parts, and the presence of a dense charge distribution on hydrophilic surfaces enables efficient capture of ions in solutions.
In this work, we performed classical molecular dynamics simulations to evaluate laminar structures formed by peptides with the (RF)(5) primary sequence. The alternating arginine (R) and phenylalanine (F) amino acids provide to the (RF)(5) peptide a facially amphipathic sheets characteristic. Experimental studies report that the (RF)(5) macromolecules can self-assembly into membrane-like or fiber-like nanostructures, however, our theoretical results indicate that the structures present more similarity with a laminar form. Our results demonstrate the existence of a dense mesh of hydrogen bonds that allows the separation of the hydrophilic and hydrophobic parts of the nanostructures in solution. Our theoretical results indicate properties that are perfectly compatible with experimental data. As an application, we noticed a dense charge distribution on the hydrophilic surfaces that allows efficient capture of ions in solutions. (C) 2021 Elsevier B.V. All rights reserved.
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