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
Molecular synergy in biolubrication: The role of cartilage oligomeric matrix protein (COMP) in surface-structuring of lubricin
KTH Royal Institute of Technology, Stockholm, Sweden.
KTH Royal Institute of Technology, Stockholm, Sweden.
KTH Royal Institute of Technology, Stockholm, Sweden.
University of Gothenburg, Gothenburg, Sweden.
Show others and affiliations
2017 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 495, 200-206 p.Article in journal (Refereed) Published
Abstract [en]

Hypothesis Synovial surfaces are lubricated by biomolecular aggregates that act in synergy, and lubricin is one key biolubricant. Its molecular structure allows extensive hydration and this is conducive to its lubrication performance. However, in order to fullfil its lubrication function it needs to be anchored and oriented on the surface in a proper way. We suggest that cartilage oligomeric matrix protein (COMP) is one of the biomolecules that promotes anchoring of lubricin in a fashion that facilitates lubrication. Experiments Weakly hydrophobic poly(methyl methacrylate) (PMMA) surfaces were coated by COMP and lubricin, individually and in combinations. Adsorption was investigated using a quartz crystal microbalance, and friction between the biopolymer-coated surfaces was determined by employing the atomic force microscope-colloidal probe technique. Findings It was found that COMP facilitated firm directed attachment of lubricin in a manner that resulted in low friction forces, significantly lower than what was achieved when lubricin was directly adsorbed to PMMA. Evidently, COMP provides means for lubricin to attach strongly and in a favourable conformation for efficient lubrication of this surface. We suggest that our findings can be extrapolated to cartilage surfaces, where co-localization of COMP and lubricin has been demonstrated.

Place, publisher, year, edition, pages
Academic Press Inc. , 2017. Vol. 495, 200-206 p.
Keyword [en]
Adsorption; Atomic force microscopy; Biomolecules; Cartilage; Esters; Friction; Oligomers; Proteins; Quartz crystal microbalances; Tribology, Cartilage surfaces; Colloidal probe techniques; COMP; Friction force; Lubrication performance; Lubricin; Poly(methyl methacrylate) (PMMA); Surface structuring, Lubrication
National Category
Chemical Engineering
Identifiers
URN: urn:nbn:se:ri:diva-30042DOI: 10.1016/j.jcis.2017.02.007Scopus ID: 2-s2.0-85012066362OAI: oai:DiVA.org:ri-30042DiVA: diva2:1119705
Available from: 2017-07-04 Created: 2017-07-04 Last updated: 2017-07-04Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textScopus
By organisation
Chemistry, Materials and Surfaces
In the same journal
Journal of Colloid and Interface Science
Chemical Engineering

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

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
v. 2.26.0