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Rheopexy of Synovial Fluid and Protein Aggregation



Katherine Oates, Wendy Krause, Ronald L. Jones, R H. Colby


Bovine synovial fluid and albumin solutions of similar concentration are rheopectic (stress increases with time in steady shear). This unusual flow characteristic is caused by protein aggrega- tion, and the total stress is enhanced by entanglement of this tenuous protein network with the long-chain polysaccharide sodium hyaluronate under physiological conditions. Neutron scattering measurements on albumin solutions demonstrate protein aggregation and all measurements are consistent with a weak dipolar attraction energy (of order 3 kT) that is most likely augmented by hydrophobic interactions and/or disulfide bond formation between proteins. Protein aggregation appears to play an important role in the mechanical properties of blood and synovial fluid. We also suggest a connection between the observed rheopexy and the remarkable lubrication properties of synovial fluid.
Journal Of The Royal Society Interface


biolubricants, hyaluronic acid, plasma proteins, rheology, small angle neutron scattering, synovial fluid


Oates, K. , Krause, W. , Jones, R. and Colby, R. (2005), Rheopexy of Synovial Fluid and Protein Aggregation, Journal Of The Royal Society Interface, [online], (Accessed June 23, 2024)


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Created September 4, 2005, Updated October 12, 2021