Structural Stability of Peptidic His-Containing Proton Wire in Solution and in the Adsorbed State

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897480" target="_blank" >RIV/60076658:12310/18:43897480 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/18:00500230 RIV/61388963:_____/18:00500230 RIV/61989592:15110/18:73588655

Výsledek na webu

<a href="https://pubs.acs.org/doi/ipdf/10.1021/acs.langmuir.7b04139" target="_blank" >https://pubs.acs.org/doi/ipdf/10.1021/acs.langmuir.7b04139</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.langmuir.7b04139" target="_blank" >10.1021/acs.langmuir.7b04139</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural Stability of Peptidic His-Containing Proton Wire in Solution and in the Adsorbed State

Popis výsledku v původním jazyce

Molecular wires are functional molecules applicable in the field of transfer processes in technological and biochemical applications. Besides molecular wires with the ability to transfer electrons, research is currently focused on molecular wires with high proton affinity and proton transfer ability. Recently, proposed peptidic proton wires (H wires) are one example. Their ability to mediate the transport of protons from aqueous solutions onto the surface of a Hg electrode in a catalytic hydrogen evolution reaction was investigated by constant-current chronopotentiometric stripping. However, elucidating the structure of H wires and rationalizing their stability are key requirements for their further research and application. In this article, we focus on the His (H) and Ala (A)-containing peptidic H wire A(3)-(H-A(2))(6) in solution and after its immobilization onto the electrode surface in the presence of the secondary structure stabilizer 2,2,2-trifluoroethanol (TFE). We found that the solvent containing more than 25% of TFE stabilizes the helical structure of A(3)-(H-A(2))(6) not only in solution but also in the adsorbed state. The TFE efficacy to stabilize alpha-helical structure was confirmed using high-resolution nuclear magnetic resonance, circular dichroism, and molecular dynamics simulation. Experimental and theoretical results indicated A3-(H-A(2))(6) to be a high proton-affinity peptidic H wire with an alpha-helical structure stabilized by TFE, which was confirmed in a comparative study with hexahistidine as an example of a peptide with a definitely disordered and random coil structure. The results presented here could be used for further investigation of the peptidic H wires and for the application of electrochemical methods in the research of proton transfer phenomena in general.

Název v anglickém jazyce

Structural Stability of Peptidic His-Containing Proton Wire in Solution and in the Adsorbed State

Popis výsledku anglicky

Molecular wires are functional molecules applicable in the field of transfer processes in technological and biochemical applications. Besides molecular wires with the ability to transfer electrons, research is currently focused on molecular wires with high proton affinity and proton transfer ability. Recently, proposed peptidic proton wires (H wires) are one example. Their ability to mediate the transport of protons from aqueous solutions onto the surface of a Hg electrode in a catalytic hydrogen evolution reaction was investigated by constant-current chronopotentiometric stripping. However, elucidating the structure of H wires and rationalizing their stability are key requirements for their further research and application. In this article, we focus on the His (H) and Ala (A)-containing peptidic H wire A(3)-(H-A(2))(6) in solution and after its immobilization onto the electrode surface in the presence of the secondary structure stabilizer 2,2,2-trifluoroethanol (TFE). We found that the solvent containing more than 25% of TFE stabilizes the helical structure of A(3)-(H-A(2))(6) not only in solution but also in the adsorbed state. The TFE efficacy to stabilize alpha-helical structure was confirmed using high-resolution nuclear magnetic resonance, circular dichroism, and molecular dynamics simulation. Experimental and theoretical results indicated A3-(H-A(2))(6) to be a high proton-affinity peptidic H wire with an alpha-helical structure stabilized by TFE, which was confirmed in a comparative study with hexahistidine as an example of a peptide with a definitely disordered and random coil structure. The results presented here could be used for further investigation of the peptidic H wires and for the application of electrochemical methods in the research of proton transfer phenomena in general.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

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>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Langmuir

ISSN

0743-7463

e-ISSN

—

Svazek periodika

34

Číslo periodika v rámci svazku

24

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

6997-7005

Kód UT WoS článku

000436022900003

EID výsledku v databázi Scopus

2-s2.0-85047393844