Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Uncovering sequence effects in Titanium binding peptides adsorption on TiO2: A molecular dynamics study
Stockholm University, Faculty of Science, Department of Chemistry.ORCID iD: 0009-0004-0000-3962
Stockholm University, Faculty of Science, Department of Chemistry.ORCID iD: 0000-0002-9390-5719
Number of Authors: 22025 (English)In: Scientific Reports, E-ISSN 2045-2322, Vol. 15, article id 26885Article in journal (Refereed) Published
Abstract [en]

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 TiO2 (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, Na+ ions playing a significant role in the anchoring of peptides to the surface. These findings suggest a detailed sequence-level understanding of peptide-TiO2 interactions and can guide the design of improved peptides for titanium functionalization.

Place, publisher, year, edition, pages
2025. Vol. 15, article id 26885
Keywords [en]
Adsorption, Molecular dynamics, Peptides, Titanium dioxide
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:su:diva-245445DOI: 10.1038/s41598-025-10966-3ISI: 001537443500019PubMedID: 40707617Scopus ID: 2-s2.0-105011494628OAI: oai:DiVA.org:su-245445DiVA, id: diva2:1989038
Available from: 2025-08-14 Created: 2025-08-14 Last updated: 2026-01-07Bibliographically approved
In thesis
1. Atomistic mechanisms and predictive modeling of biomolecular adsorption on nanomaterial surfaces
Open this publication in new window or tab >>Atomistic mechanisms and predictive modeling of biomolecular adsorption on nanomaterial surfaces
2026 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Molecular simulations provide detailed insight into how biomolecules interact with nanomaterial surfaces. However, quantitative adsorption calculations are computationally demanding, and experimental measurements alone rarely reveal the molecular mechanism of binding. This type of molecular-level understanding is often essential for guiding the design of nanomaterials with improved safety and performance in technological and medical applications. This thesis combines atomistic molecular dynamics, enhanced sampling methods, machine learning, and quartz crystal microbalance with dissipation monitoring to develop a mechanistic and predictive description of adsorption at nano-bio interfaces. Adsorption free energies were computed for a broad set of biomolecular building blocks on flat and curved ZnS nanostructures, both pristine and polymer-coated, showing how curvature, hydration structure, and polymer layers affect adsorption affinities. Building on this and on the results of previous studies, a consistently generated dataset of adsorption free energies for biomolecular fragments on various nanomaterial surfaces was analyzed using statistical machine-learning tools, revealing that biomolecules and nanomaterials cluster into a few chemically significant classes and that adsorption behavior can be reproduced using a reduced set of representative fragments in simple linear models. The thesis then shifts attention from individual fragments to short peptides, examining how the order of amino acids in a peptide sequence collectively governs adsorption behavior onto TiO2. Extensive MD simulations of sequence permutations of the titanium-binding peptide (min-TBP-1) show how the spatial arrangement of charged and polar residues, together with ion-mediated interactions, determines adsorption affinity, conformational adaptation, and preferred sequence motifs. Finally, a subset of these peptides was studied using enhanced sampling and QCM-D experiments, providing quantitative adsorption free energies and complementary information on adsorption kinetics. The comparison between computed free energies and experimentally derived binding offers a more complete picture of sequence-specific peptide adsorption. Together, these studies advance the molecular understanding of nano-bio interfaces and outline practical strategies for predicting and tailoring biomolecular adsorption on nanomaterials.

Place, publisher, year, edition, pages
Stockholm: Department of Chemistry, Stockholm University, 2026. p. 78
Keywords
Nanomaterials, ZnS, TiO2, Adsorption free energy, Molecular dynamics simulations, QCM-D
National Category
Physical Chemistry Theoretical Chemistry
Research subject
Physical Chemistry
Identifiers
urn:nbn:se:su:diva-250844 (URN)978-91-8107-486-4 (ISBN)978-91-8107-487-1 (ISBN)
Public defence
2026-02-20, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B and online via Zoom, public link is available at the department website, Stockholm, 13:00 (English)
Opponent
Supervisors
Available from: 2026-01-28 Created: 2026-01-07 Last updated: 2026-01-28Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records

Rahmani, RojaLyubartsev, Alexander P.

Search in DiVA

By author/editor
Rahmani, RojaLyubartsev, Alexander P.
By organisation
Department of Chemistry
In the same journal
Scientific Reports
Physical Chemistry

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 76 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf