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Vibrational spectroscopic and related studies of lipid/protein interaction in lung surfactant models
Descriptive
TypeOfResource
Text
TitleInfo
(ID = T-1)
Title
Vibrational spectroscopic and related studies of lipid/protein interaction in lung surfactant models
Identifier
ETD_2675
Identifier
(type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10002600001.ETD.000052954
Language
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(type = code)
English
Genre
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theses
Subject
(ID = SBJ-1);
(authority = RUETD)
Topic
Chemistry
Subject
(ID = SBJ-2);
(authority = ETD-LCSH)
Topic
Lungs--Microbiology
Subject
(ID = SBJ-3);
(authority = ETD-LCSH)
Topic
Lipids
Subject
(ID = SBJ-4);
(authority = ETD-LCSH)
Topic
Proteins
Abstract
(type = abstract)
Lung surfactant, a lipid/protein complex located at the air/alveolar lining of the mammalian lung, facilitates the work of breathing and prevents alveolar collapse. Lung surfactant associated proteins SP-A and SP-D are also involved in pulmonary innate immune response. The deficiency or dysfunction of lung surfactant may lead to pathological conditions of lungs. The "squeeze out" hypothesis was proposed in 1960s to explain the mechanism of the surface tension lowering functions of lung surfactant. It suggests that non-DPPC components are squeezed out during expiration from the monolayer and form a multilayer structure attached underneath the monolayer at high compressions. This multilayer structure serves as a surfactant reservoir to supply surfactant for the following surface expansion. Multilamellar structures have been observed in alveolar surface film and with lung surfactant models; however, its composition is not known thoroughly. In this thesis, substrate-supported films were transferred from air/water interface by a novel technique termed "COVASP", which transfers films under continuous surface compression. Model lung surfactant systems containing DPPC, DPPG, SP-C and cholesterol were used in this study. The COVASP films with a broad surface pressure coverage were characterized by IR imaging. The relative composition of multilayers was probed by the IR absorbance of characteristic vibrational modes for each component. The results showed that both phospholipids and SP-C were present in multilayers, but DPPC was concentrated to a lesser extent compared to DPPG and SP-C. The application of COVASP-IR imaging was further extended to evaluate the synthetic biomimetics of lung surfactant SP-C for potential therapeutic use. A class of N-substituted polyglycine molecules with helical structures has been synthesized as SP-C mimics by our collaborators. The ability of these peptoids to form multilayers was studied by COVASP and AFM and was compared to native SP-C. It is found that palmitoylated peptoid was able to form multilayers with lung surfactant model used, but only at a higher peptoid concentration. In addition, the extent of multilayer formation was also lower when compared to SP-C. As a component of pulmonary innate immune system, SP-A directly binds to a series of bacteria and microbes. LPS, constituents of bacterial outer membrane, are ligands of SP-A. The mode of interaction between SP-A and LPS was studied by IRRAS. It is speculated that SP-A interacted with LPS acyl chains in a Ca2+ dependent manner. Truncated SP-A was also studied and was compared to its hyperpermeabilizing mutant D215A/PL SP-A. D215A/PL SP-A was more stable at the air/water interface, which may contribute to its hyperpermeability.
PhysicalDescription
Form
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electronic resource
Extent
xvii, 159 p. : ill.
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application/pdf
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Note
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Ph.D.
Note
Includes abstract
Note
Vita
Note
(type = bibliography)
Includes bibliographical references
Note
(type = statement of responsibility)
by Guangru Mao
Name
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Mao
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Guangru
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1983-
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author
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Guangru Mao
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Mendelsohn
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Richard
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chair
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Advisory Committee
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Richard Mendelsohn
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(type = family)
He
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(type = given)
Huixin
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internal member
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Advisory Committee
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Huixin He
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(type = family)
Lalancette
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Roger
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Roger Lalancette
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Walters
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Russel M
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outside member
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Advisory Committee
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Russel M Walters
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Rutgers University
Role
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degree grantor
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Graduate School - Newark
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school
OriginInfo
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2010
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2010-05
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xx
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Title
Rutgers University Electronic Theses and Dissertations
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ETD
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Title
Graduate School - Newark Electronic Theses and Dissertations
Identifier
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rucore10002600001
Identifier
(type = doi)
doi:10.7282/T3RN37Z2
Genre
(authority = ExL-Esploro)
ETD doctoral
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Rights
RightsDeclaration
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The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder
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(type = personal)
Name
FamilyName
Mao
GivenName
Guangru
Role
Copyright Holder
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Permission or license
DateTime
2010-04-28 01:34:09
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Name
Guangru Mao
Affiliation
Rutgers University. Graduate School - Newark
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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.
RightsEvent
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Embargo
DateTime
2010-05-31
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after May 31st, 2011.
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ETD
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