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

0518366 - BFÚ 2020 RIV DE eng J - Článek v odborném periodiku
Kroutil, O. - Kabeláč, M. - Dorčák, Vlastimil - Vacek, J.
Structures of Peptidic H-wires at Mercury Surface: Molecular Dynamics Study.
Electroanalysis. Roč. 31, č. 10 (2019), s. 2032-2040. ISSN 1040-0397. E-ISSN 1521-4109
Institucionální podpora: RVO:68081707
Klíčová slova: secondary-structure * water * electrochemistry * adsorption * electrocatalysis * trifluoroethanol
Obor OECD: Analytical chemistry
Impakt faktor: 2.544, rok: 2019
Způsob publikování: Open access s časovým embargem
https://onlinelibrary.wiley.com/doi/abs/10.1002/elan.201900314

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.
Trvalý link: http://hdl.handle.net/11104/0303522