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Computational studies of peptide self-assembly
Descriptive
TitleInfo
Title
Computational studies of peptide self-assembly
Name
(type = personal)
NamePart
(type = family)
Schmidt
NamePart
(type = given)
Kassandra L.
NamePart
(type = date)
1992-
DisplayForm
Kassandra L. Schmidt
Role
RoleTerm
(authority = RULIB)
author
Name
(type = personal)
NamePart
(type = family)
Dutt
NamePart
(type = given)
Meenakshi
DisplayForm
Meenakshi Dutt
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
chair
Name
(type = personal)
NamePart
(type = family)
Olson
NamePart
(type = given)
Wilma
DisplayForm
Wilma Olson
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Nanda
NamePart
(type = given)
Vikas
DisplayForm
Vikas Nanda
Affiliation
Advisory Committee
Role
RoleTerm
(authority = RULIB)
internal member
Name
(type = corporate)
NamePart
Rutgers University
Role
RoleTerm
(authority = RULIB)
degree grantor
Name
(type = corporate)
NamePart
School of Graduate Studies
Role
RoleTerm
(authority = RULIB)
school
TypeOfResource
Text
Genre
(authority = marcgt)
theses
OriginInfo
DateCreated
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2019
DateOther
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(qualifier = exact);
(type = degree)
2019-10
Language
LanguageTerm
(authority = ISO 639-3:2007);
(type = text)
English
Abstract
(type = abstract)
Research into novel biological materials for use in biomedical applications is guided by the formation of supramolecular structures which have properties resultant from the characteristics of the compositional molecules. Peptides are commonly utilized in biological material development as their properties are widely variable and highly controllable due to the sequence-specific properties of amino acids. Self-assembling peptides are of specific interest due to their spontaneous aggregation into organized morphologies with predictable characteristics based upon their constituent amino acids. Though novel peptide materials have traditionally been researched through physical experimentation, the development of Molecular Dynamics has allowed for comparable computational studies of peptide systems. In this work, coarse-grained Molecular Dynamics simulations are selected to study self-assembling peptides from two classes, aromatic and aliphatic, as these peptides have been experimentally validated to spontaneously assemble themselves into nanostructures. Computational models representative of the peptides’ chemistry are created for aromatic peptides FF (phenylalanine-phenylalanine) and FNF (phenylalanine-asparagine-phenylalanine) and aliphatic peptides A6K (alanine-alanine-alanine-alanine-alanine-alanine-lysine), V6K (valine-valine-valine-valine-valine-valine-lysine), and V6K2 (valine-valine-valine-valine-valine-valine-lysine-lysine). In the aromatic studies, the effect of varying total peptide concentrations and relative tripeptide concentrations on the morphology of the assembled structures is characterized. In the aliphatic studies, the peptide alignment in stable aggregates and nanostructures is determined. The results demonstrate the viability of these peptide systems to form stable, usable nanostructures suitable for inclusion in biological applications that require the respective specific properties of the in-scope peptides.
Subject
(authority = RUETD)
Topic
Biomedical Engineering
Subject
(authority = local)
Topic
Molecular Dynamics
Subject
(authority = LCSH)
Topic
Peptides -- Synthesis
RelatedItem
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TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
Identifier
(type = RULIB)
ETD
Identifier
ETD_10377
PhysicalDescription
Form
(authority = gmd)
InternetMediaType
application/pdf
InternetMediaType
text/xml
Extent
1 online resource (xiv, 52 pages) : illustrations
Note
(type = degree)
M.S.
Note
(type = bibliography)
Includes bibliographical references
RelatedItem
(type = host)
TitleInfo
Title
School of Graduate Studies Electronic Theses and Dissertations
Identifier
(type = local)
rucore10001600001
Location
PhysicalLocation
(authority = marcorg);
(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/t3-0hgj-r868
Genre
(authority = ExL-Esploro)
ETD graduate
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Rights
RightsDeclaration
(ID = rulibRdec0006)
The author owns the copyright to this work.
RightsHolder
(type = personal)
Name
FamilyName
Schmidt
GivenName
Kassandra
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
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(qualifier = exact);
(point = start)
2019-09-30 13:05:32
AssociatedEntity
Name
Kassandra Schmidt
Role
Copyright holder
Affiliation
Rutgers University. School of Graduate Studies
AssociatedObject
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.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical
RULTechMD
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ContentModel
ETD
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windows xp
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1.7
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Microsoft® Word 2016
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2019-09-30T12:59:35
DateCreated
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2019-09-30T12:59:35
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