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Molecular synergy in biolubrication: The role of cartilage oligomeric matrix protein (COMP) in surface-structuring of lubricin.

Artikel i vetenskaplig tidskrift
Författare Akanksha Raj
Min Wang
Chao Liu
Liaquat Ali
Niclas G. Karlsson
Per M Claesson
Andra Dėdinaitė
Publicerad i Journal of colloid and interface science
Volym 495
Sidor 200-206
ISSN 1095-7103
Publiceringsår 2017
Publicerad vid Institutionen för biomedicin
Institutionen för biomedicin, avdelningen för medicinsk kemi och cellbiologi
Sidor 200-206
Språk en
Länkar dx.doi.org/10.1016/j.jcis.2017.02.0...
Ämnesord Adsorption, Cartilage Oligomeric Matrix Protein, chemistry, Friction, Glycoproteins, chemistry, Humans, Hyaluronic Acid, chemistry, Lubrication, Microscopy, Atomic Force, Particle Size, Polymethyl Methacrylate, chemistry, Surface Properties
Ämneskategorier Fysikalisk kemi, Cell- och molekylärbiologi


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.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.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.

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