The relation between protein adsorption and hemocompatibility of antifouling polymer brushes
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F22%3A00564084" target="_blank" >RIV/61389013:_____/22:00564084 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00023736:_____/22:00013438 RIV/60076658:12310/22:43905325
Výsledek na webu
<a href="https://onlinelibrary.wiley.com/doi/10.1002/mabi.202200247" target="_blank" >https://onlinelibrary.wiley.com/doi/10.1002/mabi.202200247</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/mabi.202200247" target="_blank" >10.1002/mabi.202200247</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The relation between protein adsorption and hemocompatibility of antifouling polymer brushes
Popis výsledku v původním jazyce
Whenever an artificial surface comes into contact with blood, proteins are rapidly adsorbed onto its surface. This phenomenon, termed fouling, is then followed by a series of undesired reactions involving activation of complement or the coagulation cascade and adhesion of leukocytes and platelets leading to thrombus formation. Thus, considerable efforts are directed towards the preparation of fouling-resistant surfaces with the best possible hemocompatibility. Herein, a comprehensive hemocompatibility study after heparinized blood contact with seven polymer brushes prepared by surface-initiated atom transfer radical polymerization is reported. The resistance to fouling is quantified and thrombus formation and deposition of blood cellular components on the coatings are analyzed. Moreover, identification of the remaining adsorbed proteins is performed via mass spectroscopy to elucidate their influence on the surface hemocompatibility. Compared with an unmodified glass surface, the grafting of polymer brushes minimizes the adhesion of platelets and leukocytes and prevents the thrombus formation. The fouling from undiluted blood plasma is reduced by up to 99%. Most of the identified proteins are connected with the initial events of foreign body reaction towards biomaterial (coagulation cascade proteins, complement component, and inflammatory proteins). In addition, several proteins that are not previously linked with blood-biomaterial interaction are presented and discussed.n
Název v anglickém jazyce
The relation between protein adsorption and hemocompatibility of antifouling polymer brushes
Popis výsledku anglicky
Whenever an artificial surface comes into contact with blood, proteins are rapidly adsorbed onto its surface. This phenomenon, termed fouling, is then followed by a series of undesired reactions involving activation of complement or the coagulation cascade and adhesion of leukocytes and platelets leading to thrombus formation. Thus, considerable efforts are directed towards the preparation of fouling-resistant surfaces with the best possible hemocompatibility. Herein, a comprehensive hemocompatibility study after heparinized blood contact with seven polymer brushes prepared by surface-initiated atom transfer radical polymerization is reported. The resistance to fouling is quantified and thrombus formation and deposition of blood cellular components on the coatings are analyzed. Moreover, identification of the remaining adsorbed proteins is performed via mass spectroscopy to elucidate their influence on the surface hemocompatibility. Compared with an unmodified glass surface, the grafting of polymer brushes minimizes the adhesion of platelets and leukocytes and prevents the thrombus formation. The fouling from undiluted blood plasma is reduced by up to 99%. Most of the identified proteins are connected with the initial events of foreign body reaction towards biomaterial (coagulation cascade proteins, complement component, and inflammatory proteins). In addition, several proteins that are not previously linked with blood-biomaterial interaction are presented and discussed.n
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10610 - Biophysics
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2022
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Macromolecular Bioscience
ISSN
1616-5187
e-ISSN
1616-5195
Svazek periodika
22
Číslo periodika v rámci svazku
11
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
13
Strana od-do
2200247
Kód UT WoS článku
000837814700001
EID výsledku v databázi Scopus
2-s2.0-85135602066