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DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide
Interactions between a solvent and their co-solute molecules in solutions of peptides are crucial for their stability and structure. The K-peptide is a synthetic fragment of a larger hen egg white lysozyme protein that is believed to be able to aggregate into amyloid structures. In this study, a com...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8836737/ https://www.ncbi.nlm.nih.gov/pubmed/35163792 http://dx.doi.org/10.3390/ijms23031872 |
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author | Godlewska, Julia Cieśla, Bartosz Wawer, Jarosław Bruździak, Piotr |
author_facet | Godlewska, Julia Cieśla, Bartosz Wawer, Jarosław Bruździak, Piotr |
author_sort | Godlewska, Julia |
collection | PubMed |
description | Interactions between a solvent and their co-solute molecules in solutions of peptides are crucial for their stability and structure. The K-peptide is a synthetic fragment of a larger hen egg white lysozyme protein that is believed to be able to aggregate into amyloid structures. In this study, a complex experimental and theoretical approach is applied to study systems comprising the peptide, water, and two co-solutes: trimethylamide N-oxide (TMAO) or dimethyl sulfoxide (DMSO). Information about their interactions in solutions and on the stability of the K-peptide was obtained by FTIR spectroscopy and differential scanning microcalorimetry. The IR spectra of various osmolyte–water–model-peptide complexes were simulated with the DFT method (B3LYP/6-311++G(d,p)). The FTIR results indicate that both solutes are neutral for the K-peptide in solution. Both co-solutes affect the peptide to different degrees, as seen in the shape of its amide I band, and have different influences on its thermal stability. DFT calculations helped simplify the experimental data for easier interpretation. |
format | Online Article Text |
id | pubmed-8836737 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88367372022-02-12 DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide Godlewska, Julia Cieśla, Bartosz Wawer, Jarosław Bruździak, Piotr Int J Mol Sci Article Interactions between a solvent and their co-solute molecules in solutions of peptides are crucial for their stability and structure. The K-peptide is a synthetic fragment of a larger hen egg white lysozyme protein that is believed to be able to aggregate into amyloid structures. In this study, a complex experimental and theoretical approach is applied to study systems comprising the peptide, water, and two co-solutes: trimethylamide N-oxide (TMAO) or dimethyl sulfoxide (DMSO). Information about their interactions in solutions and on the stability of the K-peptide was obtained by FTIR spectroscopy and differential scanning microcalorimetry. The IR spectra of various osmolyte–water–model-peptide complexes were simulated with the DFT method (B3LYP/6-311++G(d,p)). The FTIR results indicate that both solutes are neutral for the K-peptide in solution. Both co-solutes affect the peptide to different degrees, as seen in the shape of its amide I band, and have different influences on its thermal stability. DFT calculations helped simplify the experimental data for easier interpretation. MDPI 2022-02-07 /pmc/articles/PMC8836737/ /pubmed/35163792 http://dx.doi.org/10.3390/ijms23031872 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Godlewska, Julia Cieśla, Bartosz Wawer, Jarosław Bruździak, Piotr DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide |
title | DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide |
title_full | DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide |
title_fullStr | DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide |
title_full_unstemmed | DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide |
title_short | DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide |
title_sort | dmso and tmao—differences in interactions in aqueous solutions of the k-peptide |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8836737/ https://www.ncbi.nlm.nih.gov/pubmed/35163792 http://dx.doi.org/10.3390/ijms23031872 |
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