Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378271%3A_____%2F22%3A00561891" target="_blank" >RIV/68378271:_____/22:00561891 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68407700:21230/22:00353786

Výsledek na webu

<a href="https://doi.org/10.1002/cphc.202100639" target="_blank" >https://doi.org/10.1002/cphc.202100639</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cphc.202100639" target="_blank" >10.1002/cphc.202100639</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms

Popis výsledku v původním jazyce

ZnO biointerfaces with serum albumin have attracted noticeable attention due to the increasing interest in developing ZnO-based materials for biomedical applications. ZnO surface morphology and chemistry are expected to play a critical role on the structural, optical, and electronic properties of albumin-ZnO complexes. Yet there are still large gaps in the understanding of these biological interfaces. Herein we comprehensively elucidate the interactions at such interfaces by using atomic force microscopy and nanoshaving experiments to determine roughness, thickness, and adhesion properties of BSA layers adsorbed on the most typical polar and non-polar ZnO single-crystal facets. These experiments are corroborated by force field (FF) and DFTB calculations on ZnO-BSA interfaces. We show that BSA adsorbs on all the studied ZnO surfaces while interactions of BSA with ZnO are found to be considerably affected by the atomic surface structure of ZnO.n

Název v anglickém jazyce

Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms

Popis výsledku anglicky

ZnO biointerfaces with serum albumin have attracted noticeable attention due to the increasing interest in developing ZnO-based materials for biomedical applications. ZnO surface morphology and chemistry are expected to play a critical role on the structural, optical, and electronic properties of albumin-ZnO complexes. Yet there are still large gaps in the understanding of these biological interfaces. Herein we comprehensively elucidate the interactions at such interfaces by using atomic force microscopy and nanoshaving experiments to determine roughness, thickness, and adhesion properties of BSA layers adsorbed on the most typical polar and non-polar ZnO single-crystal facets. These experiments are corroborated by force field (FF) and DFTB calculations on ZnO-BSA interfaces. We show that BSA adsorbs on all the studied ZnO surfaces while interactions of BSA with ZnO are found to be considerably affected by the atomic surface structure of ZnO.n

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10305 - Fluids and plasma physics (including surface physics)

Projekt

<a href="/cs/project/GC19-02858J" target="_blank" >GC19-02858J: Přenos náboje a mikrobiologické interakce hybridních nanostruktur oxidů kovů</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

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

Název periodika

ChemPhysChem

ISSN

1439-4235

e-ISSN

1439-7641

Svazek periodika

23

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

10

Strana od-do

25-33

Kód UT WoS článku

000722264500001

EID výsledku v databázi Scopus

2-s2.0-85119672612