Adsorption of papain on solid substrates of different hydrophobicity
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F16%3A00462171" target="_blank" >RIV/61388955:_____/16:00462171 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1116/1.4958305" target="_blank" >http://dx.doi.org/10.1116/1.4958305</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1116/1.4958305" target="_blank" >10.1116/1.4958305</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Adsorption of papain on solid substrates of different hydrophobicity
Popis výsledku v původním jazyce
Adsorption properties of protein Papain at the solidjliquid (0.1M KCl) interfaces of different hydrophobicity [highly oriented pyrolytic graphite (HOPG), bare gold, CH3, OH, and COOHterminated self-assembled monolayers on gold] were studied by a combined quartz crystal microbalance and atomic force microscopy techniques. It was found that Papain forms an incomplete monolayer at hydrophobic interfaces (HOPG and CH3-terminated substrate), whereas on more hydrophilic ones, a complete monolayer formation was always observed with either the onset of the formation of a second layer (bare gold substrate) or adsorption in a multilayer fashion, possibly a bilayer formation (OH-terminated substrate). The surface concentration and compact monolayer film thickness was much lower on the COOH-terminated substrate compared to other surfaces studied. This result was explained by partial dissociation of the interfacial COOH groups leading to additional electrostatic interactions between the positively charged protein domains and negatively charged carboxylate anions, as well as to local pH changes promoting protein denaturation. © 2016 American Vacuum Society.
Název v anglickém jazyce
Adsorption of papain on solid substrates of different hydrophobicity
Popis výsledku anglicky
Adsorption properties of protein Papain at the solidjliquid (0.1M KCl) interfaces of different hydrophobicity [highly oriented pyrolytic graphite (HOPG), bare gold, CH3, OH, and COOHterminated self-assembled monolayers on gold] were studied by a combined quartz crystal microbalance and atomic force microscopy techniques. It was found that Papain forms an incomplete monolayer at hydrophobic interfaces (HOPG and CH3-terminated substrate), whereas on more hydrophilic ones, a complete monolayer formation was always observed with either the onset of the formation of a second layer (bare gold substrate) or adsorption in a multilayer fashion, possibly a bilayer formation (OH-terminated substrate). The surface concentration and compact monolayer film thickness was much lower on the COOH-terminated substrate compared to other surfaces studied. This result was explained by partial dissociation of the interfacial COOH groups leading to additional electrostatic interactions between the positively charged protein domains and negatively charged carboxylate anions, as well as to local pH changes promoting protein denaturation. © 2016 American Vacuum Society.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
CF - Fyzikální chemie a teoretická chemie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2016
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biointerphases
ISSN
1934-8630
e-ISSN
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Svazek periodika
11
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
9
Strana od-do
—
Kód UT WoS článku
000386586100004
EID výsledku v databázi Scopus
2-s2.0-84978997917