Influence of chondroitin sulfate on collagen gel structure and mechanical properties at physiologically relevant levels.
The ability to alter collagen organization could lead to more physiologically relevant scaffolds for tissue engineering. This study examined collagen organization in the presence of polysaccharide and the resulting effects on viscoelastic properties. Fibrillogenesis in the presence of chondroitin sulfate (CS) resulted in changes in the collagen network organization with an increase in void space present. The increased void space caused by CS addition correlated with a decreased stiffness of the collagen gel. These changes occurred with physiologically relevant ratios of collagen to CS, at physiological pH and ionic strength, and without a decrease in the amount of collagen incorporated into fibrils. The addition of dextran, an uncharged polysaccharide, yielded no change in network void space or mechanical properties. Changes in fibril diameter caused by CS or dextran were not correlated with mechanical properties. The results of this study demonstrate that collagen organization can be modified by the addition of GAG, leading to altered matrix mechanical properties.
Stuart
Kate
K
Purdue University, Biomedical Engineering, 206 Martin Jischke Drive, West Lafayette, Indiana 47907, USA.
Panitch
Alyssa
A
D002809:Chondroitin Sulfates / Q000737:chemistry*; D003094:Collagen / Q000737:chemistry* / Q000648:ultrastructure; D020285:Cryoelectron Microscopy; D003911:Dextrans / Q000737:chemistry; D005782:Gels / Q000737:chemistry; D006025:Glycosaminoglycans / Q000737:chemistry; D007700:Kinetics; D018613:Microscopy, Confocal; D008855:Microscopy, Electron, Scanning; D015394:Molecular Structure; D009391:Nephelometry and Turbidimetry; D012212:Rheology
D003911:Dextrans; D005782:Gels; D006025:Glycosaminoglycans; D002809:Chondroitin Sulfates; D003094:Collagen