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Molecular organization of peptide-based amphiphiles at association colloidal interfaces

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TitleInfo
Title
Molecular organization of peptide-based amphiphiles at association colloidal interfaces
Name (type = personal)
NamePart (type = family)
Zhang
NamePart (type = given)
Yongliang
NamePart (type = date)
1985-
DisplayForm
Yongliang Zhang
Role
RoleTerm (authority = RULIB)
author
Name (type = personal)
NamePart (type = family)
Romsted
NamePart (type = given)
Laurence
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Laurence Romsted
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Advisory Committee
Role
RoleTerm (authority = RULIB)
chair
Name (type = personal)
NamePart (type = family)
Warmuth
NamePart (type = given)
Ralf
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Ralf Warmuth
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Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
Jimenez
NamePart (type = given)
Leslie
DisplayForm
Leslie Jimenez
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
internal member
Name (type = personal)
NamePart (type = family)
HUANG
NamePart (type = given)
QINGRONG
DisplayForm
QINGRONG HUANG
Affiliation
Advisory Committee
Role
RoleTerm (authority = RULIB)
outside member
Name (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
TypeOfResource
Text
Genre (authority = marcgt)
theses
OriginInfo
DateCreated (qualifier = exact)
2016
DateOther (qualifier = exact); (type = degree)
2016-10
CopyrightDate (encoding = w3cdtf); (qualifier = exact)
2016
Place
PlaceTerm (type = code)
xx
Language
LanguageTerm (authority = ISO639-2b); (type = code)
eng
Abstract (type = abstract)
Elucidating proteins/peptides structures at biomembrane interface is a great challenge. We are developing a chemical approach that reveals topological information of peptides at association colloidal interfaces. This is achieved by using a UV-active amphiphilic molecular probe, a hydrophobic alkyl arenediazonium ion that is oriented with its reactive diazo headgroup in the interfacial region of association colloids and spontaneously reacts with amide bonds, reactive sidechains, and interfacial water to give products. Analysis of various tagging and fragmentation patterns provides information on the locations and local concentrations of peptide backbone and reactive sidechains within the interfacial region. In Chapter II we use this approach to estimate the local concentrations of weakly basic nucleophiles in the interfacial region of micelles of three different N-acyl amino acid amphiphiles: N-lauroylsarcosine, N-lauroylglycine and N-lauroylalanine, respectively. Our results demonstrate that the chemical probe, 4-hexadecyl-2,6-dimethyl-benzenediazonium cation, is trapped competitively and reproducibly by the amide oxygen and carboxylate groups of the amphiphile headgroup, and by water in the interfacial region of the micelles. At a bulk pH of 6.8 - 7.0, the interfacial carboxylate group molarities are estimated to be ~ 1.6 M, but the concentration of the amide bonds for C12Sar micelles is 2 - 5 times less (ca. 0.7 M) than that of C12Ala (~ 1.5 M) and C12Gly micelles (~ 3.0 M). These results indicate that the methyl group on the nitrogen of sarcosine partially buries the N-methyl amide bond in the micellar core, whereas glycine and alanine do not. In Chapter III, we run the dediazoniation reaction in a series of self-assembled di-peptide amphiphile aqueous solutions prepared at a pH range of 4.0 - 7.0. Product yields show that the local concentration of carboxylate sidechains are in the range at 1.0 - 2.5 M at a solution pH of 6 - 7, but are up to ~ 4.0 M at pH 4.5 when the dipeptide amphiphile forms a gel. Local concentrations of amide bonds are generally dependent on the peptide sequences, ranging across 1.0 - 3.0 M at a solution pH of 6 - 7, but are 2 to3 times higher at gelation pHs. In Chapter IV, a surprising minimum in the surface tension profile of sodium N-dodecanoyl sarcosinate is observed that is consistent with the literature. Our results show that the surface tension minimum in NaLS is caused in part by an excess of the protonated form of the Z-isomer. An intra-molecular hydrogen bonding interaction may exist between the amide oxygen and carboxylate headgroup of the protonated Z isomer, which contributes to its higher proton affinity than its E counterpart. Micellar dilution leads to a transfer of free acid unimer from micelles to water, concurrent with a decrease in the bulk pH.
Subject (authority = RUETD)
Topic
Chemistry and Chemical Biology
RelatedItem (type = host)
TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier (type = RULIB)
ETD
Identifier
ETD_7669
PhysicalDescription
Form (authority = gmd)
electronic resource
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (xxi, 159 p. : ill.)
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references
Subject (authority = ETD-LCSH)
Topic
Proteins
Subject (authority = ETD-LCSH)
Topic
Peptides
Subject (authority = ETD-LCSH)
Topic
Amphiphiles
Note (type = statement of responsibility)
by Yongliang Zhang
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/T3N58PQF
Genre (authority = ExL-Esploro)
ETD doctoral
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RightsDeclaration (ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder (type = personal)
Name
FamilyName
Zhang
GivenName
Yongliang
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2016-09-28 14:20:04
AssociatedEntity
Name
Yongliang Zhang
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
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License
Name
Author Agreement License
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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.
RightsEvent
DateTime (encoding = w3cdtf); (qualifier = exact); (point = start)
2016-10-31
DateTime (encoding = w3cdtf); (qualifier = exact); (point = end)
2017-05-02
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after May 2nd, 2017.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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2016-10-02T07:04:50
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2016-10-02T07:04:50
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