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An investigation of Poly (caprolactone-co-glycolide) interaction with bioactive proteins and cellular responses

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
An investigation of Poly (caprolactone-co-glycolide) interaction with bioactive proteins and cellular responses
Identifier
ETD_2524
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000053021
Language
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Pharmaceutical Science
Subject (ID = SBJ-2); (authority = ETD-LCSH)
Topic
Polymers--Testing
Subject (ID = SBJ-3); (authority = ETD-LCSH)
Topic
Crystalline polymers
Abstract (type = abstract)
The objective of the present investigation is to systematically evaluate the role of polymer crystallinity on osteoblast adhesion, proliferation, osteogenic gene expression and bioactive protein adsorption using a series of poly(caprolactone-co-glycolide) (PCL-PGA) polymers. Five compositions of pure PCL and PGA, and PCL-PGA intermediate copolymeric compositions in ratios of 25:75, 35:65 and 45:55, were selected. These polymers were fabricated into thin films by compression molding. The samples were characterized using scanning electro microscopy (SEM) for surface morphology, differential scanning caloriometry (DSC) for crystallinity, contact angle measurement for hydrophobicity (CA), and atomic force microscopy (AFM) for nanotopography. The PCL-PGA films demonstrated similar morphology, hydrophobicity and nanotopography whereas they differed significantly in crystallinity. Cell adhesion and proliferation, as well as osteogenic gene expression were evaluated with osteoblasts (HEPM 1486) on PCL-PGA surfaces. Recombinant human growth and differentiation factor 5 (rhGDF-5) and Fibronectin (Fn) were adsorbed from single protein solutions using depletion method and quantified using bicinchoninic acid (BCA) protein and radiolabelling assay. The protein-adsorbed surface nanotopography was analyzed using AFM. In the cellular responses experiments, amorphous/flexible PCL-PGA 35:65 supports osteoblast growth and promotes osteogenic gene expression significantly better than the crystalline PCL and PGA. These studies demonstrated that crystallinity and rigidity played major roles in determining cell responses with PCL-PGA polymers. Protein adsorption study results indicate that rhGDF-5 adsorbed to a higher extent on PCL surfaces and least on PGA surfaces. Reduced rhGDF-5 (a more hydrophilic and flexible protein form adsorbed significantly in greater amounts on all PCL-PGA substrates, demonstrating that the conformation and hydrophibicity of rhGDF-5 played a major role in its adsorption to PCL-PGA surfaces. Fn, a 450 kDa protein, contains multiple binding motifs with varied hydrophobicity. Binding motifs of Fn fragments strongly impacted their adsorption to PCL-PGA surfaces. The adsorption of Fn 70 kDa fragment on PCL-PGA polymers was found to favor binding to PCL material with the greatest adsorption on pure PCL surfaces, similar to the full length of Fn molecule. Collectively, these studies demonstrate that Fn (70 kda) played a major role in full-length Fn adsorption to PCL-PGA substrates.
PhysicalDescription
Form (authority = gmd)
electronic resource
Extent
xix, 184 p. : ill.
InternetMediaType
application/pdf
InternetMediaType
text/xml
Note (type = degree)
Ph.D.
Note
Includes abstract
Note
Vita
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Han Cui
Name (ID = NAME-1); (type = personal)
NamePart (type = family)
Cui
NamePart (type = given)
Han
NamePart (type = date)
1971-
Role
RoleTerm (authority = RULIB)
author
DisplayForm
Han Cui
Name (ID = NAME-2); (type = personal)
NamePart (type = family)
Sinko
NamePart (type = given)
Patrick J
Role
RoleTerm (authority = RULIB)
chair
Affiliation
Advisory Committee
DisplayForm
Patrick J Sinko
Name (ID = NAME-3); (type = personal)
NamePart (type = family)
Uhrich
NamePart (type = given)
Kathryn
Role
RoleTerm (authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Kathryn Uhrich
Name (ID = NAME-4); (type = personal)
NamePart (type = family)
Stein
NamePart (type = given)
Stanley
Role
RoleTerm (authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Stanley Stein
Name (ID = NAME-5); (type = personal)
NamePart (type = family)
Geesin
NamePart (type = given)
Jeffrey
Role
RoleTerm (authority = RULIB)
outside member
Affiliation
Advisory Committee
DisplayForm
Jeffrey Geesin
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
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/T37081JW
Genre (authority = ExL-Esploro)
ETD doctoral
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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
Cui
GivenName
Han
Role
Copyright Holder
RightsEvent (ID = RE-1); (AUTHORITY = rulib)
Type
Permission or license
DateTime
2010-04-01 17:17:01
AssociatedEntity (ID = AE-1); (AUTHORITY = rulib)
Role
Copyright holder
Name
Han Cui
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.
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Technical

ContentModel
ETD
MimeType (TYPE = file)
application/pdf
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application/x-tar
FileSize (UNIT = bytes)
3952640
Checksum (METHOD = SHA1)
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