Characterization and Biomedical Applications of Recombinant Silk-Elastinlike Protein Polymers

Persistent Link:
http://hdl.handle.net/10150/242475
Title:
Characterization and Biomedical Applications of Recombinant Silk-Elastinlike Protein Polymers
Author:
Teng, Weibing
Issue Date:
2012
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
Keywords:
Protein-Based Materials; Protein Secondary Structure; Self-Assembly; Silk-Elastin-Like Protein Polymers; Mechanical Engineering; Drug Delivery; Mechanical Characterization
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Mechanical Engineering
Degree Grantor:
University of Arizona
Advisor:
Wu, Xiaoyi

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleCharacterization and Biomedical Applications of Recombinant Silk-Elastinlike Protein Polymersen_US
dc.creatorTeng, Weibingen_US
dc.contributor.authorTeng, Weibingen_US
dc.date.issued2012-
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © 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.en_US
dc.description.releaseRelease after 30-Jul-2014en_US
dc.description.abstractBiomaterials 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.en_US
dc.typetexten_US
dc.typeElectronic Dissertationen_US
dc.subjectProtein-Based Materialsen_US
dc.subjectProtein Secondary Structureen_US
dc.subjectSelf-Assemblyen_US
dc.subjectSilk-Elastin-Like Protein Polymersen_US
dc.subjectMechanical Engineeringen_US
dc.subjectDrug Deliveryen_US
dc.subjectMechanical Characterizationen_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineMechanical Engineeringen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorWu, Xiaoyien_US
dc.contributor.committeememberWong, Pak Kinen_US
dc.contributor.committeememberZohar, Yitshaken_US
dc.contributor.committeememberYoon, Jeong-Yeolen_US
dc.contributor.committeememberWu, Xiaoyien_US
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