Flow and Aggregation of Rod-like Proteins in Slit and Cylindrical Pores Coated with Polymer Brushes: An Insight from Dissipative Particle Dynamics.

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985858%3A_____%2F17%3A00471576" target="_blank" >RIV/67985858:_____/17:00471576 - isvavai.cz</a>

Alternative codes found

RIV/44555601:13440/17:43888416

Result on the web

<a href="http://dx.doi.org/10.1039/c6sm02751b" target="_blank" >http://dx.doi.org/10.1039/c6sm02751b</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c6sm02751b" target="_blank" >10.1039/c6sm02751b</a>

Result language

angličtina

Original language name

Flow and Aggregation of Rod-like Proteins in Slit and Cylindrical Pores Coated with Polymer Brushes: An Insight from Dissipative Particle Dynamics.

Original language description

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.nThe 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.

Czech name

—

Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10403 - Physical chemistry

Project

<a href="/en/project/GA13-09914S" target="_blank" >GA13-09914S: A controlling of diffusion processes in pores with varying permeability</a><br>

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Soft Matter

ISSN

1744-683X

e-ISSN

—

Volume of the periodical

13

Issue of the periodical within the volume

8

Country of publishing house

GB - UNITED KINGDOM

Number of pages

12

Pages from-to

1634-1645

UT code for WoS article

000396026200012

EID of the result in the Scopus database

2-s2.0-85013774603