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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...

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Detalles Bibliográficos
Autores principales: Brudar, Sandi, Hribar-Lee, Barbara
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
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.
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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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