Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.

The control of protein aggregation is an important requirement in the development of bio-pharmaceutical formulations. Here a simple protein model is proposed that was used in molecular dynamics simulations to obtain a quantitative assessment of the relative contributions of proteins' net-charge...

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Autores principales:	Michael Brunsteiner, Michaela Flock, Bernd Nidetzky
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ac8e65d8ace6427499133004c2aee20a
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spelling	oai:doaj.org-article:ac8e65d8ace6427499133004c2aee20a2021-11-18T07:51:05ZStructure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.1932-620310.1371/journal.pone.0059797https://doaj.org/article/ac8e65d8ace6427499133004c2aee20a2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23565169/?tool=EBIhttps://doaj.org/toc/1932-6203The control of protein aggregation is an important requirement in the development of bio-pharmaceutical formulations. Here a simple protein model is proposed that was used in molecular dynamics simulations to obtain a quantitative assessment of the relative contributions of proteins' net-charges, dipole-moments, and the size of hydrophobic or charged surface patches to their colloidal interactions. The results demonstrate that the strength of these interactions correlate with net-charge and dipole moment. Variation of both these descriptors within ranges typical for globular proteins have a comparable effect. By comparison no clear trends can be observed upon varying the size of hydrophobic or charged patches while keeping the other parameters constant. The results are discussed in the context of experimental literature data on protein aggregation. They provide a clear guide line for the development of improved algorithms for the prediction of aggregation propensities.Michael BrunsteinerMichaela FlockBernd NidetzkyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e59797 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Michael Brunsteiner Michaela Flock Bernd Nidetzky Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
description	The control of protein aggregation is an important requirement in the development of bio-pharmaceutical formulations. Here a simple protein model is proposed that was used in molecular dynamics simulations to obtain a quantitative assessment of the relative contributions of proteins' net-charges, dipole-moments, and the size of hydrophobic or charged surface patches to their colloidal interactions. The results demonstrate that the strength of these interactions correlate with net-charge and dipole moment. Variation of both these descriptors within ranges typical for globular proteins have a comparable effect. By comparison no clear trends can be observed upon varying the size of hydrophobic or charged patches while keeping the other parameters constant. The results are discussed in the context of experimental literature data on protein aggregation. They provide a clear guide line for the development of improved algorithms for the prediction of aggregation propensities.
format	article
author	Michael Brunsteiner Michaela Flock Bernd Nidetzky
author_facet	Michael Brunsteiner Michaela Flock Bernd Nidetzky
author_sort	Michael Brunsteiner
title	Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
title_short	Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
title_full	Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
title_fullStr	Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
title_full_unstemmed	Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
title_sort	structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/ac8e65d8ace6427499133004c2aee20a
work_keys_str_mv	AT michaelbrunsteiner structurebaseddescriptorsfortheestimationofcolloidalinteractionsandproteinaggregationpropensities AT michaelaflock structurebaseddescriptorsfortheestimationofcolloidalinteractionsandproteinaggregationpropensities AT berndnidetzky structurebaseddescriptorsfortheestimationofcolloidalinteractionsandproteinaggregationpropensities
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Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities.

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