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| DOI | 10.1021/ACSOMEGA.4C10450 | ||
| Año | 2025 | ||
| Tipo |
Citas Totales
Autores Afiliación Chile
Instituciones Chile
% Participación
Internacional
Autores
Afiliación Extranjera
Instituciones
Extranjeras
The role of the cysteine-leucine-lysine (CLK) motif in enhancing the structural stability of collagen-like peptides (CLPs) adsorbed onto gold nanosurfaces is investigated in this study. The effects of CLK inclusion in CLPs on peptide adsorption, structural stability, and hydrogen bonding behavior in both solvent and surface environments are analyzed by using molecular dynamics simulations. It is shown that CLPs containing the CLK motif (P1-CLK) exhibit stronger binding, greater water displacement, and more stable conformations compared to non-modified CLPs (P1). Additionally, energetically favorable behavior is observed in simulations with multiple peptides, leading to enhanced surface coverage for P1-CLK. These findings indicate that the CLK motif is crucial for optimizing peptide-surface interactions with potential applications in biomaterials design.
| Ord. | Autor | Género | Institución - País |
|---|---|---|---|
| 1 | Galaz-Araya, Constanza | - |
Universidad de Talca - Chile
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| 2 | Galaz-Davison, Pablo | - |
Universidad de Talca - Chile
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| 3 | Cortés-Arriagada, Diego | - |
Universidad Tecnológica Metropolitana - Chile
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| 4 | Zamora, Ricardo A. | - |
Universidad de Talca - Chile
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| 5 | Poblete, Horacio | - |
Universidad de Talca - Chile
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