Protein-mediated boundary lubrication in arthroplasty

Wear of articulated surfaces can be a major lifetime-limiting factor in arthroplasty. In the natural joint, lubrication is effected by the body's natural synovial fluid. Following arthroplasty, and the subsequent reformation of the synovial membrane, a fluid of similar composition surrounds the...

Full description

Saved in:
Bibliographic Details
Published in:Biomaterials 2005-04, Vol.26 (10), p.1165-1173
Main Authors: Heuberger, M.P., Widmer, M.R., Zobeley, E., Glockshuber, R., Spencer, N.D.
Format: Article
Language:English
Subjects:
Adsorption
Albumin
Arthroplasty
Arthroplasty - methods
Binding Sites
Coated Materials, Biocompatible - chemistry
Friction
Humans
Hydrophilicity
Hydrophobic and Hydrophilic Interactions
Interface
Joint Prosthesis
Joint replacement
Kinetics
Lubrication
Materials Testing - methods
Polyethylene
Polyethylenes - chemistry
Protein adsorption
Protein Binding
Protein Conformation
Serum Albumin - chemistry
Synovial Fluid - chemistry
Temperature
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Wear of articulated surfaces can be a major lifetime-limiting factor in arthroplasty. In the natural joint, lubrication is effected by the body's natural synovial fluid. Following arthroplasty, and the subsequent reformation of the synovial membrane, a fluid of similar composition surrounds the artificial joint. Synovial fluid contains, among many other constituents, a substantial concentration of the readily adsorbing protein albumin. The ability of human serum albumin to act as a boundary lubricant in joint prostheses has been investigated using a pin-on-disc tribometer. Circular dichroism spectroscopy was employed to follow the temperature- and time-dependent conformational changes of human serum albumin in the model lubricant solution. Effects of protein conformation and polymer surface hydrophilicity on protein adsorption and the resulting friction in the boundary lubrication regime have been investigated. Unfolded proteins preferentially adsorb onto hydrophobic polymer surfaces, where they form a compact, passivating layer and increase sliding friction—an effect that can be largely suppressed by rendering the substrate more hydrophilic. A molecular model for protein-mediated boundary friction is proposed to consolidate the observations. The relevance of the results for in vivo performance and ex vivo hip-joint testing are discussed.
ISSN:0142-9612
1878-5905
DOI:10.1016/j.biomaterials.2004.05.020