Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • 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
AFM Study of pH-Dependent Adhesion of Single Protein to TiO2 Surface
Luleå University of Technology, Department of Engineering Sciences and Mathematics, Energy Science. State Key Laboratory of Materials-Oriented and Chemical Engineering Nanjing Tech University.
Department of Materials and Environmental Chemistry Arrhenius Laboratory Stockholm University. Centre of Advanced Research in Bionanoconjugates and Biopolymers Petru Poni Institute of Macromolecular Chemistry Aleea Grigore Ghica-Voda, Iasi, Romania. State Key Laboratory of Materials-Oriented and Chemical Engineering Nanjing Tech University, China.
State Key Laboratory of Tribology Tsinghua University, Beijing, China.
Luleå University of Technology, Department of Engineering Sciences and Mathematics, Energy Science.ORCID iD: 0000-0002-0200-9960
Show others and affiliations
2019 (English)In: Advanced Materials Interfaces, ISSN 2196-7350, Vol. 6, no 14, article id 1900411Article in journal (Refereed) Published
Abstract [en]

The effect of pH-induced electrostatic conditions on the molecular interaction force of a single lysozyme molecule with TiO2 is investigated using atomic force microscopy (AFM). The force between the charged or neutral lysozyme molecule and the TiO2 surface is measured at different pH from 3.6 to 10.8. It is found to be directly proportional to the contact area, given by an effective diameter of the lysozyme molecule, and is further qualitatively verified by the AFM-measured friction coefficients. The results of the Derjaguin–Landau–Verwey–Overbeek theory show that the pH can change the surface charge densities of both lysozyme and TiO2, but the molecular interaction force at different pH is only dependent on the pH-induced effective diameter of lysozyme. The molecular interaction forces, quantified at the nanoscale, can be directly used to design high-performance liquid chromatography measurements at macroscale by tuning the retention time of a protein under varied pH conditions. They can also be applied to develop a model for predicting and controlling the chromatographic separations of proteins.

Place, publisher, year, edition, pages
John Wiley & Sons, 2019. Vol. 6, no 14, article id 1900411
Keywords [en]
AFM, DLVO theory, electrostatic conditions, HPLC, molecular interaction force
National Category
Energy Engineering
Research subject
Energy Engineering
Identifiers
URN: urn:nbn:se:ltu:diva-74601DOI: 10.1002/admi.201900411ISI: 000478624200016Scopus ID: 2-s2.0-85067084518OAI: oai:DiVA.org:ltu-74601DiVA, id: diva2:1325716
Note

Validerad;2019;Nivå 2;2019-08-21 (johcin)

Available from: 2019-06-17 Created: 2019-06-17 Last updated: 2019-08-21Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textScopus

Authority records BETA

Dong, YihuiJi, Xiaoyan

Search in DiVA

By author/editor
Dong, YihuiJi, Xiaoyan
By organisation
Energy Science
In the same journal
Advanced Materials Interfaces
Energy Engineering

Search outside of DiVA

GoogleGoogle Scholar

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 23 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • 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