Insight into peculiar adhesion of cells to plasma-chemically prepared multifunctional "amino-glue" surfaces

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26620%2F23%3APU148450" target="_blank" >RIV/00216305:26620/23:PU148450 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/00216224:14310/23:00131232 RIV/44555601:13440/23:43897694

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/10.1002/ppap.202200157" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/ppap.202200157</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/ppap.202200157" target="_blank" >10.1002/ppap.202200157</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Insight into peculiar adhesion of cells to plasma-chemically prepared multifunctional "amino-glue" surfaces

Popis výsledku v původním jazyce

Plasma polymers (PPs) can easily modify material surfaces to improve their bio-applicability due to match-made surface-free energy and functionality. However, cell adhesion to PPs typically composed of various functional groups has not yet been fully understood. We explain the origin of strong resistance to trypsin treatment previously noted for nonendothelial cells on amine PPs. It is caused mainly by nonspecific adhesion of negatively charged parts of transmembrane proteins to the positively charged amine PP surface, enabled by thin glycocalyx. However, endothelial cells are bound primarily by their thick, negatively charged glycocalyx and sporadically by integrins in kinetic traps, both cleaved by trypsin. Cell scratching by atomic force microscopy tip confirmed the correlation of trypsin resistance to the strength of cell adhesion.

Název v anglickém jazyce

Insight into peculiar adhesion of cells to plasma-chemically prepared multifunctional "amino-glue" surfaces

Popis výsledku anglicky

Plasma polymers (PPs) can easily modify material surfaces to improve their bio-applicability due to match-made surface-free energy and functionality. However, cell adhesion to PPs typically composed of various functional groups has not yet been fully understood. We explain the origin of strong resistance to trypsin treatment previously noted for nonendothelial cells on amine PPs. It is caused mainly by nonspecific adhesion of negatively charged parts of transmembrane proteins to the positively charged amine PP surface, enabled by thin glycocalyx. However, endothelial cells are bound primarily by their thick, negatively charged glycocalyx and sporadically by integrins in kinetic traps, both cleaved by trypsin. Cell scratching by atomic force microscopy tip confirmed the correlation of trypsin resistance to the strength of cell adhesion.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10300 - Physical sciences

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2023

Kód důvěrnosti údajů

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

Název periodika

Plasma Processes and Polymers

ISSN

1612-8850

e-ISSN

1612-8869

Svazek periodika

20

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

15

Strana od-do

1-15

Kód UT WoS článku

000941082700001

EID výsledku v databázi Scopus

2-s2.0-85149387367