Interaction of graphene oxide with albumins: Effect of size, pH, and temperature
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216305%3A26620%2F16%3APU118806" target="_blank" >RIV/00216305:26620/16:PU118806 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.abb.2016.02.015" target="_blank" >http://dx.doi.org/10.1016/j.abb.2016.02.015</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.abb.2016.02.015" target="_blank" >10.1016/j.abb.2016.02.015</a>
Alternative languages
Result language
angličtina
Original language name
Interaction of graphene oxide with albumins: Effect of size, pH, and temperature
Original language description
Understanding the interaction between graphene oxide (GO) and the biomolecules is fundamentally essential, especially for disease- and drug-related peptides and proteins. In this study, the interaction between GO and albumins (bovine serum albumin, human serum albumin, and bovine alpha-lactalbumin) has been performed by fluorescence and UV–Vis spectroscopic techniques. The fluorescence quenching mechanism between GO and aromatic acids residues with intrinsic fluorescence was determined as mainly static quenching in combination with dynamic quenching. The optimal conditions for the most effective affinity between albumins and GO have been estimated at neutral pH and room temperature. The strong impact of the size of graphene oxide on the interaction between proteins and graphene oxide has been confirmed, as well. The interaction between GO and albumins has been examined as electrostatic and hydrophobic. The electrostatic interaction was confirmed by pH effect, while the hydrophobic interaction was proved by the presence of Poloxamer188. The CD spectra of albumins exhibit decreasing helicity in the secondary structure of albumins upon the addition of GO. However, no significant changes in position and shape of characteristic negative bands have been noted. Mentioned changes indicate the successful interaction between GO and proteins, the predominantly α-helical structure of albumins has been preserved.
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
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
ISSN
0003-9861
e-ISSN
1096-0384
Volume of the periodical
593
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
69-79
UT code for WoS article
000371751400007
EID of the result in the Scopus database
2-s2.0-84958170493