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Chemical and biomolecular functionalization of silicon surfaces for biosensing applications

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
Chemical and biomolecular functionalization of silicon surfaces for biosensing applications
Identifier
ETD_1787
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000051369
Language
LanguageTerm (authority = ISO639-2)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Biomedical Engineering
Subject (ID = SBJ-1); (authority = ETD-LCSH)
Topic
Surface chemistry
Subject (ID = SBJ-1); (authority = ETD-LCSH)
Topic
Silicon
Subject (ID = SBJ-1); (authority = ETD-LCSH)
Topic
Biosensors
Abstract
The reliable functioning of biosensors and bioassays is dependent on the robust attachment of active biomolecules to device substrates, such that the structural integrity, organization and appropriate orientation of these molecules at the surface is maintained. To a significant extent, the underlying surface chemistry and molecular organization that these biomolecules come in contact with and attach to affect the properties of the functional overlayer that they compose. In this work, primarily through the use of infrared spectroscopy, we characterize two main types of biosensor platforms including biotin-streptavidin linkage and surface attachment and covalent attachment of protein to sensor surfaces via amines and sulfhydryls. We further observe the effects of several variations in processing conditions on these platforms including initial atmospheric humidity, use of anhydrous versus aqueous solvents in molecular adsorption and the effect of primary molecular layer stability on the organization and characteristics of subsequently adsorbed biolayers.
With infrared spectroscopy, not only do we identify the formation and breaking of chemical bonds in each of the attachment steps, we also monitor changes in the moieties of each layer with changing environmental conditions. We find that changes in ureido moiety vibrational modes of the biotinylated surface occur near 1250 and 1700 cm-1 dependent on the stability of an underlying layer of aminopropyltriethoxysiloxane, on the type of solvent used in biotinylation itself, and on subsequent protein adsorption to and/or rinsing of the biotinylated surface. In covalent attachment studies, we use small molecules in lieu of protein to characterize amine and sulfhydryl chemical bonding to maleimide-terminated surfaces and using infrared polarization techniques, we find that molecular orientation may be restricted upon covalent attachment. Ellipsometry is used in conjuction with infrared absorption area measurements to determine the relative composition of silane and maleimide prior to attachment of protein.
Additionally, fluorescence measurements of labeled protein are used to quantify protein desorption by surface acoustic wave streaming (SAWS). These measurements are correlated with power dose of SAWS operation. In all, these surface characterization methods are found to successfully monitor chemical and biomolecular layer formation and change under a variety of conditions.
PhysicalDescription
Form (authority = gmd)
electronic resource
Extent
xiii, 192 p. : ill.
InternetMediaType
application/pdf
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text/xml
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Note (type = statement of responsibility)
by Norman A. Lapin
Name (ID = NAME-1); (type = personal)
NamePart (type = family)
Lapin
NamePart (type = given)
Norman A.
NamePart (type = date)
1974
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author
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Norman A. Lapin
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Chabal
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Yves
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chair
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Advisory Committee
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Yves J. Chabal
Name (ID = NAME-3); (type = personal)
NamePart (type = family)
Yarmush
NamePart (type = given)
Martin
Role
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internal member
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Advisory Committee
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Martin Yarmush
Name (ID = NAME-4); (type = personal)
NamePart (type = family)
Kim
NamePart (type = given)
Sobin
Role
RoleTerm (authority = RULIB); (type = )
internal member
Affiliation
Advisory Committee
DisplayForm
Sobin Kim
Name (ID = NAME-5); (type = personal)
NamePart (type = family)
Ludescher
NamePart (type = given)
Richard
Role
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outside member
Affiliation
Advisory Committee
DisplayForm
Richard D. Ludescher
Name (ID = NAME-1); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB); (type = )
degree grantor
Name (ID = NAME-2); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB); (type = )
school
OriginInfo
DateCreated (point = ); (qualifier = exact)
2009
DateOther (qualifier = exact); (type = degree)
2009-05
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
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NjNbRU
Identifier (type = doi)
doi:10.7282/T3R49QZZ
Genre (authority = ExL-Esploro)
ETD doctoral
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
RightsEvent (AUTHORITY = rulib); (ID = 1)
Type
Permission or license
Detail
Non-exclusive ETD license
AssociatedObject (AUTHORITY = rulib); (ID = 1)
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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ETD
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application/pdf
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application/x-tar
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3645440
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