Galaz-Araya Constanza, Galaz-Davison Pablo, Cortés-Arriagada Diego, Zamora Ricardo A, Poblete Horacio
Departamento de Bioinformática, Centro de Bioinformática, Simulación y Modelado (CBSM), Facultad de Ingeniería, Campus Talca, Universidad de Talca, 2 Norte 685, Talca 3465548, Chile.
Programa Institucional de Fomento a la Investigación, Desarrollo e Innovación, Universidad Tecnológica Metropolitana, Ignacio Valdivieso 2409, P.O. Box 8940577, San Joaquín, Santiago 8330383, Chile.
ACS Omega. 2025 Mar 6;10(10):10366-10374. doi: 10.1021/acsomega.4c10450. eCollection 2025 Mar 18.
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.
本研究探讨了半胱氨酸 - 亮氨酸 - 赖氨酸（CLK）基序在增强吸附于金纳米表面的类胶原肽（CLPs）结构稳定性方面的作用。通过分子动力学模拟分析了CLK基序包含在CLPs中对肽吸附、结构稳定性以及在溶剂和表面环境中的氢键行为的影响。结果表明，与未修饰的CLPs（P1）相比，含有CLK基序的CLPs（P1-CLK）表现出更强的结合力、更大的水置换能力和更稳定的构象。此外，在多个肽的模拟中观察到能量上有利的行为，导致P1-CLK的表面覆盖率增加。这些发现表明，CLK基序对于优化肽 - 表面相互作用至关重要，在生物材料设计中具有潜在应用。
