Interaction of graphene oxide with albumins: Effect of size, pH, and temperature

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Interaction of graphene oxide with albumins: Effect of size, pH, and temperature

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Interaction of graphene oxide with albumins: Effect of size, pH, and temperature

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

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

2016

Kód důvěrnosti údajů

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

Název periodika

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

ISSN

0003-9861

e-ISSN

1096-0384

Svazek periodika

593

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

69-79

Kód UT WoS článku

000371751400007

EID výsledku v databázi Scopus

2-s2.0-84958170493