Uncovering sequence effects in Titanium binding peptides adsorption on TiO2: A molecular dynamics study

Abstract 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 pept...

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Bibliographic Details
Main Authors: Roja Rahmani, Alexander P. Lyubartsev
Format: Article
Language:English
Published: Nature Portfolio 2025-07-01
Series:Scientific Reports
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Online Access:https://doi.org/10.1038/s41598-025-10966-3
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Summary:Abstract 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 $$\hbox {TiO}_2$$ (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, $$\hbox {Na}^{+}$$ ions playing a significant role in the anchoring of peptides to the surface. These findings suggest a detailed sequence-level understanding of peptide- $$\hbox {TiO}_{2}$$ interactions and can guide the design of improved peptides for titanium functionalization.
ISSN:2045-2322