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    Characterization and Biomedical Applications of Recombinant Silk-Elastinlike Protein Polymers

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    Author
    Teng, Weibing
    Issue Date
    2012
    Keywords
    Protein-Based Materials
    Protein Secondary Structure
    Self-Assembly
    Silk-Elastin-Like Protein Polymers
    Mechanical Engineering
    Drug Delivery
    Mechanical Characterization
    Advisor
    Wu, Xiaoyi
    
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    Publisher
    The University of Arizona.
    Rights
    Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
    Embargo
    Release after 30-Jul-2014
    Abstract
    Biomaterials requirements nowadays are becoming more and more specialized to meet increasingly demanding needs for biomedical applications such as matrices for tissue scaffolds. Among various useful classes of biomaterials, protein-based materials have been extensively pursued as they can offer a wide range of material properties to accommodate a broader spectrum of functional and performance requirements. The advent of genetic engineering and recombinant DNA technology has enabled the production of new protein-based biopolymers with precisely controlled amino acid sequence. As an example, silk-elastinlike protein (SELP) polymers consisting of polypeptide sequences from native silk of remarkable mechanical strength and polypeptide sequences from native elastin that is extremely durable and resilient have been produced. In this dissertation, a particular silk-elastinlike protein copolymer, SELP-47K, was cast into film form, and fully characterized for its material properties, including the mechanical property, secondary structure transition, optical transparency, surface, and other physical, chemical properties. The relationship between mechanical property and protein secondary structure was investigated as well. In addition, the material property tunability which can be induced by physical, mechanical, and chemical treatments has been explored. It is worth noting that the physically crosslinked SELP-47K films displayed mechanical properties comparable to those of native elastin obtained from bovine ligament. Secondary structure study through Raman and FTIR spectra showed that methanol treatment is capable of inducing theβ-sheet crystallization of silklike blocks, which act as physical crosslinks in the protein polymer chain network, thus stabilizing the protein structure and conferring the improved material integrity. The SELP-47K protein polymer thin films displayed excellent optical transparency. In particular, its excellent optical transmittance (over 90%) in visible light range may indicate SELPs can be a family of promising biomaterial candidate for ocular applications. Besides material property characterization, SELP-47K protein polymer has been fabricated into a variety of drug delivery devices to sustainably release a common ocular antibiotic, ciprofloxacin over a period of up to 220 h, with near-first order kinetics.
    Type
    text
    Electronic Dissertation
    Degree Name
    Ph.D.
    Degree Level
    doctoral
    Degree Program
    Graduate College
    Mechanical Engineering
    Degree Grantor
    University of Arizona
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