CLK基序对吸附在金纳米表面的类胶原肽结构稳定性影响的分子动力学研究。

IF 4.3 3区化学 Q2 CHEMISTRY, MULTIDISCIPLINARY

ACS Omega Pub Date : 2025-03-06 eCollection Date: 2025-03-18 DOI:10.1021/acsomega.4c10450

Constanza Galaz-Araya, Pablo Galaz-Davison, Diego Cortés-Arriagada, Ricardo A Zamora, Horacio Poblete

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引用次数: 0

摘要

本研究探讨了半胱氨酸-亮氨酸-赖氨酸（CLK）基序在增强吸附在金纳米表面的胶原样肽（CLPs）结构稳定性中的作用。通过分子动力学模拟分析了CLK包合在CLPs中对多肽在溶剂和表面环境中的吸附、结构稳定性和氢键行为的影响。结果表明，与未修饰的CLPs （P1）相比，含有CLK基序的CLPs （P1-CLK）具有更强的结合、更大的水位移和更稳定的构象。此外，在多肽的模拟中观察到能量有利的行为，导致P1-CLK的表面覆盖增强。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的应用前景。

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Molecular Dynamics Study on the Influence of the CLK Motif on the Structural Stability of Collagen-Like Peptides Adsorbed on Gold Nanosurfaces.

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.

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来源期刊

ACS Omega Chemical Engineering-General Chemical Engineering

CiteScore

6.60

自引率

4.90%

发文量

3945

审稿时长

2.4 months

期刊介绍： ACS Omega is an open-access global publication for scientific articles that describe new findings in chemistry and interfacing areas of science, without any perceived evaluation of immediate impact.