Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager-Fuoss theory

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10124377" target="_blank" >RIV/00216208:11310/12:10124377 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/12:00376619

Výsledek na webu

<a href="http://dx.doi.org/10.1002/elps.201100602" target="_blank" >http://dx.doi.org/10.1002/elps.201100602</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/elps.201100602" target="_blank" >10.1002/elps.201100602</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager-Fuoss theory

Popis výsledku v původním jazyce

We investigated the effect of the background electrolyte (BGE) anions on the electrophoretic mobilities of the cationic amino acids arginine and lysine and the polycationic peptides tetraarginine, tetralysine, nonaarginine, and nonalysine. BGEs composedof sodium chloride, sodium propane-1,3-disulfonate, and sodium sulfate were used. For the amino acids, determination of the limiting mobility by extrapolation, using the OnsagerFuoss (OF) theory expression, yielded consistent estimates. For the peptides,however, the estimates of the limiting mobilities were found to spuriously depend on the BGE salt. This paradox was resolved using molecular modeling. Simulations, on all-atom as well as coarse-grained levels, show that significant counterion condensation, an effect not accounted for in OF theory, occurs for the tetra- and nonapeptides, even for low BGE concentrations. Including this effect in the quantitative estimation of the BGE effect on mobility removed the discrepancy between the

Název v anglickém jazyce

Counterion condensation in short cationic peptides: Limiting mobilities beyond the Onsager-Fuoss theory

Popis výsledku anglicky

We investigated the effect of the background electrolyte (BGE) anions on the electrophoretic mobilities of the cationic amino acids arginine and lysine and the polycationic peptides tetraarginine, tetralysine, nonaarginine, and nonalysine. BGEs composedof sodium chloride, sodium propane-1,3-disulfonate, and sodium sulfate were used. For the amino acids, determination of the limiting mobility by extrapolation, using the OnsagerFuoss (OF) theory expression, yielded consistent estimates. For the peptides,however, the estimates of the limiting mobilities were found to spuriously depend on the BGE salt. This paradox was resolved using molecular modeling. Simulations, on all-atom as well as coarse-grained levels, show that significant counterion condensation, an effect not accounted for in OF theory, occurs for the tetra- and nonapeptides, even for low BGE concentrations. Including this effect in the quantitative estimation of the BGE effect on mobility removed the discrepancy between the

Druh

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

CEP obor

CF - Fyzikální chemie a teoretická chemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F08%2F0114" target="_blank" >GA203/08/0114: Specifické iontové efekty pro proteiny v roztocích a podobné biologicky relevantní systémy.</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Electrophoresis

ISSN

0173-0835

e-ISSN

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Svazek periodika

33

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

981-989

Kód UT WoS článku

000303155700012

EID výsledku v databázi Scopus

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