| Autor: |
Rahali, Seyfeddine, Damous, Maamar, Belhocine, Youghourta, Sbei, Najoua, Said, Ridha Ben, Diawara, Moussa, Seydou, Mahamadou |
| Předmět: |
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| Zdroj: |
Theoretical Chemistry Accounts: Theory, Computation, & Modeling; Feb2024, Vol. 143 Issue 2, p1-11, 11p |
| Abstrakt: |
The current work investigated the interaction of ZnO nanoparticles (NPs) with glycine, tyrosine, methionine and phenylalanine. (ZnO)12 cage-like cluster was modeled using the density functional theory to determine the adsorption energy, the preferred sites for adsorption of amino acids, and the electronic structure of the formed complexes. The findings suggest that pure amino acids interact with (ZnO)12 via a chemisorption process. The thermodynamic parameters computed showed that the complexation is an exothermic process and enthalpy-driven. The oxygen atoms in the carboxyl groups of the four studied amino acids are involved in the adsorption process. PHE_Zn12O12 exhibits the highest adsorption energy (− 207.50 kJ/mol) due to its interaction with the Zn12O12 nanocluster through two different adsorption sites. The electronic and sensing properties were examined by analyzing the HOMO and LUMO energies and the HOMO–LUMO energy gap (|ΔEg|). The sensitivity of Zn12O12 nanocluster toward the studied amino acids was examined by comparing the percentage variation of the gap after the adsorption, which can reach the value of 38%, suggesting the potential of Zn12O12 nanocluster as a promising sensor for the detection of amino acids. Interaction region indicator (IRI) analysis was performed for a visual understanding of the different interactions occurring between the amino acids and the Zn12O12 nanocluster. The results of this study can shed some light on the possible application of ZnO-based nanobiosensors for detecting protein tyrosine/tryptophan nitration as an early symptom of several serious chronic diseases. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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