Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms
The result's identifiers
Result code in 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>
Alternative codes found
RIV/68407700:21230/22:00353786
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Strong structural and electronic binding of bovine serum albumin to ZnO via specific amino acid residues and zinc atoms
Original language description
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
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10305 - Fluids and plasma physics (including surface physics)
Result continuities
Project
<a href="/en/project/GC19-02858J" target="_blank" >GC19-02858J: Charge transfer and microbiological interactions of hybrid metal oxide nanostructures</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ChemPhysChem
ISSN
1439-4235
e-ISSN
1439-7641
Volume of the periodical
23
Issue of the periodical within the volume
2
Country of publishing house
DE - GERMANY
Number of pages
10
Pages from-to
25-33
UT code for WoS article
000722264500001
EID of the result in the Scopus database
2-s2.0-85119672612