Characterization of gels composed of blends of collagen I, collagen III, and chondroitin sulfate.
Type I collagen is explored heavily for use in biomaterials, but the role of other extracellular matrix components in regulating collagen organization is gaining attention. We show that as the ratio of type III to type I collagen increases, fibril diameter decreases. A mixture of the two collagen types results in a more open structural network, corresponding to a more compliant material, as compared to a material composed of only one collagen type. Glycosaminoglycans also affect collagen organization and tissue properties. We show that chondroitin sulfate decreases the collagen fibril diameter. Additionally, chondroitin sulfate (CS) increases the void space of a collagen I or collagen III gel, resulting in a more compliant material, but the interactions between types I and III collagen negate the effects of CS. The simple combination of these components results in materials with unique structural, mechanical, and biological cues that can be useful in tailoring biomaterials for tissue engineering.
Stuart
Kate
K
Weldon School of Biomedical Engineering, Purdue University, 206 South Martin Jischke Drive, West Lafayette, Indiana 47907, USA.
Panitch
Alyssa
A
D001665:Binding Sites; D001672:Biocompatible Materials / Q000737:chemistry; D002809:Chondroitin Sulfates / Q000737:chemistry*; D024042:Collagen Type I / Q000737:chemistry*; D024061:Collagen Type III / Q000737:chemistry*; D005782:Gels / Q000737:chemistry; D006025:Glycosaminoglycans / Q000737:chemistry; D010316:Particle Size; D012212:Rheology; D013499:Surface Properties
D001672:Biocompatible Materials; D024042:Collagen Type I; D024061:Collagen Type III; D005782:Gels; D006025:Glycosaminoglycans; D002809:Chondroitin Sulfates