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

Kód výsledku v IS VaVaI

RIV/67985858:_____/17:00471576 - isvavai.cz

Nalezeny alternativní kódy

RIV/44555601:13440/17:43888416

Výsledek na webu

http://dx.doi.org/10.1039/c6sm02751b

DOI - Digital Object Identifier

10.1039/c6sm02751b

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

GA13-09914S: Studium difuzních procesů v porézních látkách s proměnnou propustností

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Soft Matter

ISSN

1744-683X

e-ISSN

—

Svazek periodika

13

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

12

Strana od-do

1634-1645

Kód UT WoS článku

000396026200012

EID výsledku v databázi Scopus

2-s2.0-85013774603