Staff View
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 (ID = T-1)
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
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (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.
PhysicalDescription
Form (authority = gmd)
electronic resource
Extent
xxvi, 150 p. : ill.
InternetMediaType
application/pdf
InternetMediaType
text/xml
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = vita)
Includes vita
Note (type = statement of responsibility)
by Arnold Luk
Name (ID = NAME-1); (type = personal)
NamePart (type = family)
Luk
NamePart (type = given)
Arnold
Role
RoleTerm (authority = RULIB)
author
DisplayForm
Arnold Luk
Name (ID = NAME-2); (type = personal)
NamePart (type = family)
Kohn
NamePart (type = given)
Joachim
Role
RoleTerm (authority = RULIB)
chair
Affiliation
Advisory Committee
DisplayForm
Joachim Kohn
Name (ID = NAME-3); (type = personal)
NamePart (type = family)
Mann
NamePart (type = given)
Adrian
Role
RoleTerm (authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Adrian Mann
Name (ID = NAME-4); (type = personal)
NamePart (type = family)
Roth
NamePart (type = given)
Charles
Role
RoleTerm (authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Charles Roth
Name (ID = NAME-5); (type = personal)
NamePart (type = family)
Latour
NamePart (type = given)
Robert
Role
RoleTerm (authority = RULIB)
outside member
Affiliation
Advisory Committee
DisplayForm
Robert Latour
Name (ID = NAME-1); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (ID = NAME-2); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
OriginInfo
DateCreated (qualifier = exact)
2010
DateOther (qualifier = exact); (type = degree)
2010-10
Place
PlaceTerm (type = code)
xx
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Location
PhysicalLocation (authority = marcorg); (displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier (type = doi)
doi:10.7282/T3H41R5V
Genre (authority = ExL-Esploro)
ETD doctoral
Back to the top

Rights

RightsDeclaration (AUTHORITY = GS); (ID = rulibRdec0006)
The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder (ID = PRH-1); (type = personal)
Name
FamilyName
Luk
GivenName
Arnold
Role
Copyright Holder
RightsEvent (ID = RE-1); (AUTHORITY = rulib)
Type
Permission or license
DateTime
2010-06-18 19:31:50
AssociatedEntity (ID = AE-1); (AUTHORITY = rulib)
Role
Copyright holder
Name
Arnold Luk
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject (ID = AO-1); (AUTHORITY = rulib)
Type
License
Name
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.
Back to the top

Technical

ContentModel
ETD
MimeType (TYPE = container)
application/x-tar
FileSize (UNIT = bytes)
2457600
Checksum (METHOD = SHA1)
cdf9fa84a2aa0d5c4bcf035b44373eee4d8f7c59
MimeType (TYPE = file)
application/pdf
Back to the top
Version 8.3.13
Rutgers University Libraries - Copyright ©2021