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Viscoelastic properties of proteoglycan solutions with varying proportions present as aggregates
Author(s) -
Hardingham T. E.,
Muir H.,
Kwan M. K.,
Lai W. M.,
Mow V. C.
Publication year - 1987
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100050107
Subject(s) - proteoglycan , viscoelasticity , rheology , shear rate , materials science , chemistry , viscosity , shear modulus , shear stress , shear (geology) , chromatography , chemical engineering , biophysics , composite material , extracellular matrix , biochemistry , engineering , biology
Monomer and aggregated proteoglycans were prepared from piglaryngeal cartilage. Vascoelastic flow properties, comprising linear complex dynamic shear modulus, nonlinear steady‐state shear‐rate dependent viscosity, and primary normal stress difference, were measured in proteoglycan solutions containing varying proportions of aggregate (0–80%) and at different concentrations (10–50 mg/ml). Results were analyzed using the simple Oldroyd four‐parameter nonlinear rate‐type rheological equation. All solution properties were strongly dependent on proteoglycan concentration and on the proportion of aggregates present. Aggregation was found to have a great effect on the zero shear‐rate viscosity at 50 mg/ml, which increased fivefold from 0–100% aggregate. The results showed that network formation in proteoglycan solutions increased with concentration from 10–50 mg/ml and also increased with aggregation. All proteoglycan solutions showed shear thinning, which was most marked with aggregated proteoglycan at high concentration (50 mg/ml), where the viscosity decreased tenfold from the zero shear‐rate limit to the infinite shear‐rate limit. The intermolecular interactions in the network were therefore increasingly disrupted by increasing shear rate, but repeated measurements showed that these were reversible changes and that testing did not induce disaggregation or degradation of proteoglycan. These rheological properties show that aggregation is likely to immobilize proteoglycan at high concentration within cartilage and to contribute to the material properties of the porous solid matrix of articular cartilage that are important for its load‐bearing function.