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

Area of Science:

• Materials Science and Engineering
• Biotechnology
• Nanotechnology

Background:

• Titanium-binding peptides are crucial for functionalizing materials in biomedical and nanotechnology fields due to their selective titanium surface adhesion.
• Understanding peptide-surface interactions is key to optimizing material properties and applications.

Purpose of the Study:

• To investigate the adsorption behavior of permuted titanium-binding peptides on hydroxylated anatase titanium dioxide surfaces.
• To identify specific peptide sequences exhibiting enhanced adsorption affinity to titanium surfaces.
• To elucidate the atomic-level interactions governing peptide-titanium binding.

Main Methods:

• Utilized extensive atomistic molecular dynamics (MD) simulations.
• Analyzed 360 distinct six-amino-acid peptide sequences derived from permutations of the RKLPDA residue sequence.
• Employed clustering and radial distribution function (RDF) analyses to characterize binding modes and interactions.

Main Results:

• Minor alterations in amino acid sequence significantly impact peptide binding strength and conformational stability.
• Peptides with N-terminal arginine and C-terminal lysine or aspartic acid demonstrated more stable adsorption.
• Key interactions involved nitrogen-containing groups and titanium ions, influencing peptide anchoring to the surface.

Conclusions:

• Provides a detailed, sequence-level understanding of peptide-titanium dioxide interactions.
• Findings can guide the rational design of novel peptides with improved affinity for titanium functionalization.
• Highlights the potential for tailored peptide sequences in advanced material applications.