Author
Weyers, Amanda; Linhardt, Robert J.
Other Contributors
Date Issued
2013-05-01
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Neoproteoglycans in tissue engineering, A. Weyers, R. J. Linhardt, FEBS Journal, 280, 2511–2522, 2013.
Abstract
Proteoglycans, comprised of a core protein to which glycosaminoglycan chains are covalently linked, are an important structural and functional family of macromolecules found in the extracellular matrix. Advances in our understanding of biological interactions have lead to a greater appreciation for the need to design tissue engineering scaffolds that incorporate mimetics of key extracellular matrix components. A variety of synthetic and semisynthetic molecules and polymers have been examined by tissue engineers that serve as structural, chemical and biological replacements for proteoglycans. These proteoglycan mimetics have been referred to as neoproteoglycans and serve as functional and therapeutic replacements for natural proteoglycans that are often unavailable for tissue engineering studies. Although neoproteoglycans have important limitations, such as limited signaling ability and biocompatibility, they have shown promise in replacing the natural activity of proteoglycans through cell and protein binding interactions. This review focuses on the recent in vivo and in vitro tissue engineering applications of three basic types of neoproteoglycan structures, protein-glycosaminoglycan conjugates, nano-glycosaminoglycan composites and polymer-glycosaminoglycan complexes.;
Description
FEBS Journal, 280, 2511–2522; Note : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Publisher
FEBS Press
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; FEBS Journal; https://harc.rpi.edu/;
Access
A full text version is available in DSpace@RPI;