Interactions of nanobubbles with bovine serum albumin and papain films on gold surfaces

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F11%3A00371755" target="_blank" >RIV/61388955:_____/11:00371755 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1116/1.3650300" target="_blank" >http://dx.doi.org/10.1116/1.3650300</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1116/1.3650300" target="_blank" >10.1116/1.3650300</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Interactions of nanobubbles with bovine serum albumin and papain films on gold surfaces

Popis výsledku v původním jazyce

Nanobubbles formed on monocrystalline gold/water interface by means of the ethanol-to-water solvent exchange were exposed to the solutions of either bovine serum albumin or papain proteins. Both proteins do not change the position of nanobubbles in water, as observed by in situ tapping mode atomic force microscopy imaging before and after the introduction of the protein. The aqueous environment was subsequently replaced by ethanol. While all nanobubbles were found to dissolve in ethanol in the presenceof bovine serum albumin, most of them survived when papain was employed. The protective ability of papain was ascribed to its resistance towards the protein denaturation in aqueous solutions of ethanol. The authors employed in situ atomic force nanolithography to investigate the nanomorphology of the papain/nanobubble assemblies in ethanol.

Název v anglickém jazyce

Interactions of nanobubbles with bovine serum albumin and papain films on gold surfaces

Popis výsledku anglicky

Nanobubbles formed on monocrystalline gold/water interface by means of the ethanol-to-water solvent exchange were exposed to the solutions of either bovine serum albumin or papain proteins. Both proteins do not change the position of nanobubbles in water, as observed by in situ tapping mode atomic force microscopy imaging before and after the introduction of the protein. The aqueous environment was subsequently replaced by ethanol. While all nanobubbles were found to dissolve in ethanol in the presenceof bovine serum albumin, most of them survived when papain was employed. The protective ability of papain was ascribed to its resistance towards the protein denaturation in aqueous solutions of ethanol. The authors employed in situ atomic force nanolithography to investigate the nanomorphology of the papain/nanobubble assemblies in ethanol.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CG - Elektrochemie

OECD FORD obor

—

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)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

BIOINTERPHASES

ISSN

1559-4106

e-ISSN

—

Svazek periodika

6

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

164-170

Kód UT WoS článku

000298966600006

EID výsledku v databázi Scopus

—