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The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions
The effect of arginine on the phase stability of the hen egg-white lysozyme (HEWL) has been studied via molecular dynamics computer simulations, as well as experimentally via cloud-point temperature determination. The experiments show that the addition of arginine increases the stability of the HEWL...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9861001/ https://www.ncbi.nlm.nih.gov/pubmed/36674727 http://dx.doi.org/10.3390/ijms24021197 |
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author | Brudar, Sandi Hribar-Lee, Barbara |
author_facet | Brudar, Sandi Hribar-Lee, Barbara |
author_sort | Brudar, Sandi |
collection | PubMed |
description | The effect of arginine on the phase stability of the hen egg-white lysozyme (HEWL) has been studied via molecular dynamics computer simulations, as well as experimentally via cloud-point temperature determination. The experiments show that the addition of arginine increases the stability of the HEWL solutions. The computer simulation results indicate that arginine molecules tend to self-associate. If arginine residues are located on the protein surface, the free arginine molecules stay in their vicinity and prevent the way protein molecules “connect” through them to form clusters. The results are not sensitive to a particular force field and suggest a possible microscopic mechanism of the stabilizing role of arginine as an excipient. |
format | Online Article Text |
id | pubmed-9861001 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98610012023-01-22 The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions Brudar, Sandi Hribar-Lee, Barbara Int J Mol Sci Article The effect of arginine on the phase stability of the hen egg-white lysozyme (HEWL) has been studied via molecular dynamics computer simulations, as well as experimentally via cloud-point temperature determination. The experiments show that the addition of arginine increases the stability of the HEWL solutions. The computer simulation results indicate that arginine molecules tend to self-associate. If arginine residues are located on the protein surface, the free arginine molecules stay in their vicinity and prevent the way protein molecules “connect” through them to form clusters. The results are not sensitive to a particular force field and suggest a possible microscopic mechanism of the stabilizing role of arginine as an excipient. MDPI 2023-01-07 /pmc/articles/PMC9861001/ /pubmed/36674727 http://dx.doi.org/10.3390/ijms24021197 Text en © 2023 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 Brudar, Sandi Hribar-Lee, Barbara The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions |
title | The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions |
title_full | The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions |
title_fullStr | The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions |
title_full_unstemmed | The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions |
title_short | The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions |
title_sort | effect of arginine on the phase stability of aqueous hen egg-white lysozyme solutions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9861001/ https://www.ncbi.nlm.nih.gov/pubmed/36674727 http://dx.doi.org/10.3390/ijms24021197 |
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