Design of synthetic peptidoglycans that bind type III collagen
Abstract
The organization of type I collagen and how it is affected by glycosaminoglycans (GAGs), proteoglycans (PGs), and other extracellular matrix (ECM) components have been extensively studied. Type III collagen and its interactions with GAGs and PGs have not been widely studied. Small leucine-rich proteoglycans (SLRPs) are found incorporated in all collagenous tissues and have been shown to modulate collagen fibrillogenesis. In a previous study, type I collagen-binding peptidoglycans were synthesized to mimic the native SLRP decorin. Synthetic peptidoglycans consist of a collagen-binding peptide attached to a GAG chain, such as dermatan sulfate (DS). This study examines the effects of type III collagen-binding peptidoglycans on collagen organization. The effects of two peptidoglycans, DS-KELNLVYTGC and DS-GSITTIDVPWNVGC, on type III collagen fibrillogenesis, morphology, viscoelastic properties, and biological properties are assessed in this study. These peptidoglycans affect the fibril diameter and density, enhance the viscoelastic properties, and alter the biological properties of type III collagen gels. The ability to control the organization of type III collagen demonstrates the tissue engineering application of peptidoglycans. Type I collagen has been widely studied as a biomaterial for varied tissue engineering applications. The prevalence of type III collagen in vascular tissue indicates that it may be an advantageous component of tissue engineered blood vessels. Future work may investigate vascular tissue engineering materials consisting of types I and III collagen in the presence of synthetic collagen-binding peptidoglycans.
Degree
M.S.B.M.E.
Advisors
Panitch, Purdue University.
Subject Area
Biomedical engineering
Off-Campus Purdue Users:
To access this dissertation, please log in to our
proxy server.