Site Home
Contact Us
å

iDEA: DREXEL LIBRARIES E-REPOSITORY AND ARCHIVES

iDEA: DREXEL LIBRARIES E-REPOSITORY AND ARCHIVES

Main sections

Electrospinning Crosslinked Gelatin, Collagen, and Elastin Nanofibers for Tissue Engineering Applications

Details
Title
Electrospinning Crosslinked Gelatin, Collagen, and Elastin Nanofibers for Tissue Engineering Applications
Author(s)
Sutherland, Bryan Patrick
Advisor(s)
Schauer, Caroline L.
Keywords
Materials science; Electrospinning; Crosslinked polymers; Collagen
Date
2014-06
Publisher
Drexel University
Thesis
M.S., Materials Science and Engineering -- Drexel University, 2014
Abstract
Over 1.3 million Americans are affected by rheumatoid arthritis, a disorder in which the immune system enzymatically degrades the bodys extracellular matrices (ECM). Collagen and elastin are important components in ECMs that interact to provide both structure and flexibility to cells. Using these naturally-derived polymers as tissue engineering scaffolds is advantageous due to their inherent biocompatibility. Processing these materials using electrospinning is a suitable method of producing an environment similar to natural ECM and allowing cells to grow and proliferate. However, using these materials as scaffolds requires the fibrous mats to be insoluble in order to retain their structure, avoid enzymatic degradation, and allow cells to grow in an aqueous environment. Chemical crosslinkers, such as divinylsulfone (DVS) epichlorohydrin (ECH), genipin (GEN), and hexamethylene-1,6- di(aminocarboxysulfonate) (HDACS), were utilized as a means to create a scaffolding material that wont dissolve in water. Gelatin, the hydrolyzed form of collagen, was also tested in the same manner as collagen in order to compare the effectiveness of the crosslinking between the polymer systems. Fibers of gelatin and collagen were electrospun in a 9:1 acetic acid:water solution and produced uniform cylindrical fibers with respective diameters of 12729 nm and 11629 nm. With the addition of crosslinking molecules to the system, it was seen that the fiber diameters increased as much as six times for gelatin, while collagen fibers only increased by up to one-half time. Solubility measurements showed that GEN was the most successful crosslinking molecule causing gelatin fibers to retain some fiber morphology after 72 h at pH 7. Collagen samples crosslinked with GEN remained intact, but completely filmed after 72 h at pH 7. It is likely due to the inaccessibility of some reaction sites caused by the fibril structure of the collagen molecule. This work enhances the future applications of crosslinked gelatin, collagen, and elastin nanofibers in the field of rheumatoid arthritis and other tissue engineering applications.
URI
http://hdl.handle.net/1860/4498
In Collections
Theses, Dissertations, and Projects

Search iDEA

Advanced Search