Glycosaminoglycans (GAGs) are molecules that govern the load-bearing and frictional properties of cartilage and the lubricating properties of synovial fluid of joints. Most GAGs in the body form proteoglycans (PGs), and the dominant PG in cartilage is the bottlebrush-shaped aggrecan, comprised of a protein core decorated by GAG side chains consisting mainly of chondroitin sulfate (CS) and keratan sulfate. Additionally, hyaluronic acid (HA) induces aggrecan to self-assemble into complexes having up to 100 aggrecan molecules attached to each HA chain "backbone". Here, we report the rheological properties of CS, HA, aggrecan, and aggrecan-HA complexes in water and salt solutions. We find that CS solutions are viscous liquids, while HA solutions exhibit viscoelasticity and shear thinning. Specifically, in the case of HA, the storage modulus G' exceeds the loss modulus G '' at high frequencies (omega) while the reverse is true at low.. Thus, the rheologies of CS and HA exhibit somewhat distinct viscoelastic properties omega Aggrecan, on the other hand, shows a rheology consistent with an incipient "weak gel" in which G' and G '' cross at a specific. and follow a power-law scaling over a wide. range. Moreover, aggrecan samples do not attain an observable plateau in the viscosity under steady shear and low shear rates. Finally, the complexation of aggrecan and HA over a period of 48 h results in a slow evolution ("aging") in measured rheological properties, with G' at low omega progressively increases in time, while G '' remains essentially unchanged. This suggests that aggrecan and HA gradually form a macroscopic network in which molecular complexes act as physical cross-links.