Collagen fibrillogenesis is a multistep process involving assembly of molecules into fibrils and bundles of fibrils. The exact role of proteoglycans in collagen fibrillogenesis is unclear. The purpose of these studies is to study the effect of proteoglycans on collagen fibrillogenesis in vitro. Results of these studies suggest that the proteoglycans dermatan sulphate and chondroitin sulphate do not change the final turbidity and hence the diameter of fibrils formed during the early stages of fibrillogenesis. This suggests that proteoglycans may not influence the early phases of collagen assembly, such as nucleation. However, proteoglycans added during the final stages of collagen fibre formation in vitro cause changes in ultimate tensile strength. In the presence of the high-molecular-weight proteoglycan, the ultimate tensile strength is increased by a factor of 1.5 above that of the control, whilst in the presence of low-molecular weight chondroitin sulphate proteoglycan the tensile strength is significantly decreased. It is concluded that proteoglycans influence the later stages of fibre formation. The presence of high-molecular-weight chondroitin sulphate proteoglycan leads to efficient stress transfer between collagen fibrils, altering the ultimate tensile strength. The results of these studies will be useful in optimizing the design of collagen tendon-ligament prostheses.
All Science Journal Classification (ASJC) codes
- Ceramics and Composites
- Mechanics of Materials
- Collagen fibres