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Flow and Aggregation of Rod-like Proteins in Slit and Cylindrical Pores Coated with Polymer Brushes: An Insight from Dissipative Particle Dynamics.
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SYSNO ASEP 0471576 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Flow and Aggregation of Rod-like Proteins in Slit and Cylindrical Pores Coated with Polymer Brushes: An Insight from Dissipative Particle Dynamics. Author(s) Posel, Zbyšek (UCHP-M) RID, ORCID, SAI
Svoboda, Martin (UCHP-M) RID, SAI, ORCID
Colina, C.M. (US)
Lísal, Martin (UCHP-M) RID, ORCID, SAISource Title Soft Matter - ISSN 1744-683X
Roč. 13, č. 8 (2017), s. 1634-1645Number of pages 12 s. Language eng - English Country GB - United Kingdom Keywords chains ; dendrimers ; glycoproteins Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry R&D Projects GA13-09914S GA ČR - Czech Science Foundation (CSF) Institutional support UCHP-M - RVO:67985858 UT WOS 000396026200012 EID SCOPUS 85013774603 DOI 10.1039/c6sm02751b Annotation We use a meso-scale dissipative particle dynamics method to simulate the flow and aggregation of rodlike protein solutions through pores grafted with a solvent-sensitive polymer brush. The coated pores can control protein permeability and aggregation by a stretch-to-collapse conformational transition of the brush polymers in response to changes in the solvent quality. The protein solutions mimic aqueous glycoprotein solutions and proteins are represented as rod-like objects formed by coarse-grain beads.
The model further employs two types of beads to represent the existence of cystein-like terminal groups in real glycoproteins and mimic the aggregation of real glycoproteins in aqueous solutions. We vary the solvent quality with respect to the brush chains and study the flow and aggregation of rod-like proteins in the slit and cylindrical pores as the brush polymers undergo the stretch-to-collapse transition. The results show that stretched brush chains close the pore, hamper proteins’ flow and promote proteins’ aggregation. The collapsed brush chains open the pores for proteins’ flow and suppress their aggregation. Therefore, we observe more than a ten-fold reduction in the permeation rate of proteins in both pore geometries. Finally, due to pore confinement, larger proteins’ aggregates are formed in the slit pore than in the cylindrical pore, while more pronounced orientation of proteins in the flow direction is seen in the cylindrical pore than in the slit pore.Workplace Institute of Chemical Process Fundamentals Contact Eva Jirsová, jirsova@icpf.cas.cz, Tel.: 220 390 227 Year of Publishing 2017
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