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Excellent Protein Immobilization and Stability on Heterogeneous C–TiO2 Hybrid Nanostructures: A Single Protein AFM Study
State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing 210009, P.R. China.
Luleå University of Technology, Department of Engineering Sciences and Mathematics, Energy Science.ORCID iD: 0000-0002-0200-9960
State Key Laboratory of Materials-Oriented Chemical Engineering, Nanjing Tech University, Nanjing 210009, P.R. China. Department of Materials and Environmental Chemistry, Arrhenius Laboratory, Stockholm University, SE-10691 Stockholm, Sweden. Centre of Advanced Research in Bionanoconjugates and Biopolymers, Petru Poni Institute of Macromolecular Chemistry, Aleea Grigore Ghica-Voda, 41A, 700487 Iasi, Romania.ORCID iD: 0000-0001-9783-4535
School of Chemistry, Tel Aviv University, Tel Aviv 69978, Israel.
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2020 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 36, no 31, p. 9323-9332Article in journal (Refereed) Published
Abstract [en]

Enhancing molecular interaction is critical for improving the immobilization and stability of proteins on TiO2 surfaces. In this work, mesoporous TiO2 materials with varied pore geometries were decorated with phenyl phosphoric acid (PPA), followed by a thermal treatment to obtain chemically heterogeneous C–TiO2 samples without changing the geometry and crystalline structure, which can keep the advantages of both carbon and TiO2. The molecular interaction force between the protein and the surfaces was measured using atomic force microscopy by decomposing from the total adhesion forces, showing that the surface chemistry determines the interaction strength and depends on the amount of partial carbon coverage on the TiO2 surface (∼40–80%). Samples with 58.3% carbon coverage provide the strongest molecular interaction force, consistent with the observation from the detected friction force. Surface-enhanced Raman scattering and electrochemical biosensor measurements for these C–TiO2 materials were further conducted to illustrate their practical implications, implying their promising applications such as in protein detection and biosensing.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2020. Vol. 36, no 31, p. 9323-9332
National Category
Energy Engineering
Research subject
Energy Engineering
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URN: urn:nbn:se:ltu:diva-80577DOI: 10.1021/acs.langmuir.0c01942ISI: 000562137700032PubMedID: 32673488Scopus ID: 2-s2.0-85089606995OAI: oai:DiVA.org:ltu-80577DiVA, id: diva2:1461542
Note

Validerad;2020;Nivå 2;2020-08-27 (alebob)

Available from: 2020-08-27 Created: 2020-08-27 Last updated: 2021-03-24Bibliographically approved

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Ji, XiaoyanLaaksonen, Aatto

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