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Collagen fibrillogenesis is modulated by biomimetic proteoglycans
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Collagen fibrillogenesis is modulated by biomimetic proteoglycans

Tao Yang
Master of Science (M.S.), Drexel University
Mar 2016
DOI:
https://doi.org/10.17918/00008266
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Abstract

Collagen Extracellular Matrix Materials Science
Collagen is one of the leading components in extracellular matrix (ECM), proving durability, structural integrity, and functionality for many tissues. Deregulation of collagen fibrillogenesis and excessive collagen degradation of many interstitial connective tissues have been associated with a number of dysfunctions and diseases. Recently, we developed a novel, biocompatible, semisynthetic biomimetic proteoglycan (BPG), which consists of an enzymatically resistant synthetic polymer core and natural chondroitin sulfate bristles arranged in a three-dimensional bottle-brush configuration similar to natural aggrecan. We demonstrated that BPGl 0 (~180 BCDa) is an effective factor to regulate type I collagen fibrillogenesis, reflected by its efficient regulatory role in controlling the end-to-end fusion and lateral growth during collagen fibril formation. In addition, the network structure of formed fibrils could be modulated by the presence of BPGl 0 significantly. Similarly, BPG250 ( -2000 KDa) did affect the collagen self-assembly but it was less effective than BPGIO. Structural property of collagen scaffolds could be modulated by two proteoglycan mimic, suggesting endogenous ECM could be structural altered by incorporation of a synthetic proteoglycan without a core protein.

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