Rahmani Roja, Lyubartsev Alexander P
Department of Chemistry, Stockholm University, Svante Arrhenius väg 16C, Stockholm, 10691, Sweden.
Sci Rep. 2025 Jul 24;15(1):26885. doi: 10.1038/s41598-025-10966-3.
Titanium binding peptides are useful tools for material functionalization in both biomedical and nanotechnology applications because of their ability to attach selectively to titanium surfaces. In this work, we investigate the adsorption behavior of a series of 360 six amino acids long peptides obtained by permutations of titanium binding peptide residues, RKLPDA, on hydroxylated anatase [Formula: see text] (101) surfaces using extensive atomistic molecular dynamics (MD) simulations, with the purpose identifying sequences with stronger adsorption affinity to titanium. Our results show that small changes in amino acid order can significantly affect both binding strength and structural conformations. Peptides with arginine at the N-terminus and lysine or aspartic acid near the C-terminus tended to exhibit more stable adsorption. The clustering and radial distribution function (RDF) analyzes revealed different binding modes and key atomic interactions, with nitrogen-containing groups and, in some cases, [Formula: see text] ions playing a significant role in the anchoring of peptides to the surface. These findings suggest a detailed sequence-level understanding of peptide-[Formula: see text] interactions and can guide the design of improved peptides for titanium functionalization.
钛结合肽因其能够选择性地附着在钛表面，成为生物医学和纳米技术应用中材料功能化的有用工具。在这项工作中，我们使用广泛的原子分子动力学（MD）模拟，研究了一系列通过钛结合肽残基RKLPDA的排列获得的360个六氨基酸长的肽在羟基化锐钛矿[公式：见文本]（101）表面上的吸附行为，目的是识别对钛具有更强吸附亲和力的序列。我们的结果表明，氨基酸顺序的微小变化会显著影响结合强度和结构构象。N端为精氨酸且C端附近为赖氨酸或天冬氨酸的肽往往表现出更稳定的吸附。聚类和径向分布函数（RDF）分析揭示了不同的结合模式和关键原子相互作用，含氮基团以及在某些情况下的[公式：见文本]离子在肽与表面的锚定中起重要作用。这些发现为肽与[公式：见文本]相互作用提供了详细的序列水平理解，并可指导设计用于钛功能化的改进肽。
