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Poly(DTE-co-PEG Carbonate) as a model system for investigating the effects of physicochemical polymer characteristics on protein adsorption and cell attachment
Descriptive
TypeOfResource
Text
TitleInfo
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Title
Poly(DTE-co-PEG Carbonate) as a model system for investigating the effects of physicochemical polymer characteristics on protein adsorption and cell attachment
Identifier
ETD_2759
Identifier
(type = hdl)
http://hdl.rutgers.edu/1782.1/rucore10001600001.ETD.000056517
Language
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eng
Genre
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theses
Subject
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(authority = RUETD)
Topic
Biomedical Engineering
Subject
(ID = SBJ-2);
(authority = ETD-LCSH)
Topic
Proteins--Absorption and adsorption
Subject
(ID = SBJ-3);
(authority = ETD-LCSH)
Topic
Cytology
Subject
(ID = SBJ-4);
(authority = ETD-LCSH)
Topic
Apoptosis
Subject
(ID = SBJ-5);
(authority = ETD-LCSH)
Topic
Neutrons--Scattering
Subject
(ID = SBJ-6);
(authority = ETD-LCSH)
Topic
Hysteresis
Abstract
(type = abstract)
Protein adsorption is a complex phenomenon that is governed by chemical, physical, and thermodynamic factors. It is one of the first events to occur upon implantation of a biomaterial, and can modulate both the initial and long-term cellular response. The control of protein adsorption through modifications in material chemistry has been a subject of great interest for several decades. Poly(ethylene glycol) (PEG) is often copolymerized with other biomedical polymers to reduce protein adsorption. However, the thermodynamic incompatibility stemming from copolymerization of a highly hydrophilic polymer such as PEG with a copolymer often results in phase separation. The spatial distribution of phase-separated structures may allow for protein adsorption to occur even in PEG-containing polymers. Physical properties that affect phase separation, such as polymer molecular weight and polydispersity, may also play a role in further modifying protein adsorption behavior. To study the physicochemical factors that modulate phase separation and subsequent protein adsorption and cell attachment, a model random multiblock hydrophobic-hydrophilic copolymer system consisting of desaminotyrosyl-tyrosine ethyl ester (DTE) as the hydrophobic component and PEG as the hydrophilic component was investigated. The effect of systematic changes in PEG molecular weight and PEG composition on phase separation was explored. The spatial effects of phase separation on protein adsorption were examined using proteins with different dimensions. Additional changes in physicochemical properties were achieved by isolating specific molecular weight chains from certain polymer compositions. Finally, the effects of phase separation on cell attachment and spreading were examined. Variations in PEG content and molecular weight produced clear, systematic changes in the spatial distribution of hydrophobic and hydrophilic regions within each polymer composition. The effects of phase separation were initially inconclusively linked to protein adsorption behavior. However, variations in polymer molecular weight and chain distribution within certain polymer compositions appear to modulate protein adsorption capabilities. Phase separation also appears to play a significant role in cell attachment and spreading. While intermediate amounts of PEG repelled cells and proteins, high amounts of PEG caused cells to increase spreading on the polymeric substrates. The increased spreading was linked to dynamic overexpression of integrin α5 over time. The results of this study elucidate additional design parameters in the rational design of biomaterials, and also suggest that intermediate amounts of PEG may be optimal for developing cell-repellent surfaces.
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electronic resource
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xxvi, 150 p. : ill.
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Ph.D.
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Includes bibliographical references
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Includes vita
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by Arnold Luk
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Luk
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Arnold
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Arnold Luk
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Kohn
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Joachim
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Joachim Kohn
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Mann
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Adrian
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internal member
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Adrian Mann
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Roth
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Charles
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Charles Roth
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Latour
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Robert
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Robert Latour
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Rutgers University
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Graduate School - New Brunswick
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school
OriginInfo
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2010
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2010-10
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xx
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Title
Rutgers University Electronic Theses and Dissertations
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ETD
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Graduate School - New Brunswick Electronic Theses and Dissertations
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rucore19991600001
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doi:10.7282/T3H41R5V
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ETD doctoral
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Rights
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder
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Name
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Luk
GivenName
Arnold
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Copyright Holder
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Permission or license
DateTime
2010-06-18 19:31:50
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Name
Arnold Luk
Affiliation
Rutgers University. Graduate School - New Brunswick
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Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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