Structures of Peptidic H-wires at Mercury Surface: Molecular Dynamics Study

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00518366" target="_blank" >RIV/68081707:_____/19:00518366 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/19:43899736 RIV/61989592:15110/19:73596142

Výsledek na webu

<a href="https://onlinelibrary.wiley.com/doi/abs/10.1002/elan.201900314" target="_blank" >https://onlinelibrary.wiley.com/doi/abs/10.1002/elan.201900314</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/elan.201900314" target="_blank" >10.1002/elan.201900314</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structures of Peptidic H-wires at Mercury Surface: Molecular Dynamics Study

Popis výsledku v původním jazyce

Biopolymer immobilization strategies, self-assembly systems and adsorption phenomenon in general are crucial for the development of methods that work on the basis of the surface-detection principle, including electrochemistry. A mechanistic view into the interaction of biopolymers with electrode surfaces is also important for studying fundamental and dynamic processes such as electron/proton transport. In this sense, the utilization of new approaches for investigating the interfacial behavior of immobilized biomolecular architectures is a permanent focus. Here we use a molecular dynamics (MD) approach to simulate the structural changes and metallic surface interactions of a model 21-mer peptide of His (H) and Ala (A), A(3)(HA(2))(6), a peptidic proton wire (H-wire). This H-wire was previously proposed for the electrochemical study of proton transfer at mercury electrodes (Langmuir, 2018, 34, 6997). The rigid solid mercury mono-atomic layer (alpha-mercury lattice model) was used systematically in all our simulations. The calculations were performed in a simulation box with 1, 16 and 32 H-wire strands attached covalently to the mercury layer via the thiol group of a cysteinamide residue appended to the H-wire C-terminus. The internal alpha-helical configuration of H-wires was maintained by the presence of 2,2,2-trifluoroethanol. It was shown that both the surface density of H-wires and the protonation state of His residues play a decisive role in the structural stability and orientation of the peptide to the surface, whereas the applied voltage only has a mild effect on it, especially in case of 16 and 32 H-wire strand configurations. The MD simulations presented here could be used for the further investigation of other peptides at metallic surfaces and for electrochemical analyses of structural changes of surface-attached peptides that depend on their protonation states and other external factors.

Název v anglickém jazyce

Structures of Peptidic H-wires at Mercury Surface: Molecular Dynamics Study

Popis výsledku anglicky

Biopolymer immobilization strategies, self-assembly systems and adsorption phenomenon in general are crucial for the development of methods that work on the basis of the surface-detection principle, including electrochemistry. A mechanistic view into the interaction of biopolymers with electrode surfaces is also important for studying fundamental and dynamic processes such as electron/proton transport. In this sense, the utilization of new approaches for investigating the interfacial behavior of immobilized biomolecular architectures is a permanent focus. Here we use a molecular dynamics (MD) approach to simulate the structural changes and metallic surface interactions of a model 21-mer peptide of His (H) and Ala (A), A(3)(HA(2))(6), a peptidic proton wire (H-wire). This H-wire was previously proposed for the electrochemical study of proton transfer at mercury electrodes (Langmuir, 2018, 34, 6997). The rigid solid mercury mono-atomic layer (alpha-mercury lattice model) was used systematically in all our simulations. The calculations were performed in a simulation box with 1, 16 and 32 H-wire strands attached covalently to the mercury layer via the thiol group of a cysteinamide residue appended to the H-wire C-terminus. The internal alpha-helical configuration of H-wires was maintained by the presence of 2,2,2-trifluoroethanol. It was shown that both the surface density of H-wires and the protonation state of His residues play a decisive role in the structural stability and orientation of the peptide to the surface, whereas the applied voltage only has a mild effect on it, especially in case of 16 and 32 H-wire strand configurations. The MD simulations presented here could be used for the further investigation of other peptides at metallic surfaces and for electrochemical analyses of structural changes of surface-attached peptides that depend on their protonation states and other external factors.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

<a href="/cs/project/LTAUSA17163" target="_blank" >LTAUSA17163: Molekulární simulace procesů na rozhraní pevná látka - kapalina</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2019

Kód důvěrnosti údajů

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

Název periodika

Electroanalysis

ISSN

1040-0397

e-ISSN

—

Svazek periodika

31

Číslo periodika v rámci svazku

10

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

9

Strana od-do

2032-2040

Kód UT WoS článku

000479714500001

EID výsledku v databázi Scopus

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