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Developing tools to study the interaction between the lipopeptide surfactin and phospholipid bicelles with infrared spectroscopy

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dc.contributor.authorBlaser, Jennifer M., author
dc.contributor.authorKrummel, Amber, advisor
dc.contributor.authorLevinger, Nancy, committee member
dc.contributor.authorKipper, Matthew, committee member
dc.date.accessioned2007-01-03T08:11:19Z
dc.date.available2013-09-01T08:10:42Z
dc.date.issued2012
dc.description.abstractSurfactin has been shown to have concentration-dependent effects on lipid membranes with proposed mechanisms of action including ion chelation, ion channel formation, and a detergent-like effect. The concentration ranges for these behaviors have not been established, the structure of surfactin in a membrane has not been determined, and information regarding the dynamics of the surfactin-lipid interaction is limited at best. Therefore, a tunable phospholipid bicelle system was created to study the surfactin-lipid interaction as a function of surfactin concentration using infrared (IR) spectroscopy which can provide both structural and dynamic information. But first, the direct interaction between surfactin and bicelles was confirmed with dynamic light scattering (DLS) measurements that suggest surfactin exhibits detergent-like effects above a 2.0 mM concentration. For surfactin in Tris buffer, the IR spectra displayed a significant concentration-dependent shift in the amide-I band and a distinct change in the amide-I to amide-II band intensity ratio. These data indicate that surfactin experiences a conformational transition over the concentration range studied. The conformational transition may occur due to the formation of surfactin micelles and higher order aggregates upon increasing concentration. Surfactin was also studied in the presence of phospholipid bicelles. At low surfactin concentrations in the presence of bicelles, the amide-I band exhibits nearly identical spectral features to those found for higher concentrations of surfactin in Tris buffer, and the amide-I to amide-II band intensity ratios showed similar trends. The results of these studies indicate that the conformation of surfactin may be similar in micelles, higher order aggregates, and bicelles with the bicelles limiting the conformational distribution of the surfactin molecules. Additional studies are necessary to determine surfactin's structure in these model membranes and obtain dynamic information to better understand the mechanism of the surfactin-lipid interaction.
dc.format.mediumborn digital
dc.format.mediummasters theses
dc.identifierBlaser_colostate_0053N_11256.pdf
dc.identifierETDF2012500263CHEM
dc.identifier.urihttp://hdl.handle.net/10217/68155
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.subjectbicelles
dc.subjectsurfactin
dc.subjectspectroscopy
dc.titleDeveloping tools to study the interaction between the lipopeptide surfactin and phospholipid bicelles with infrared spectroscopy
dc.typeText
dcterms.embargo.expires2013-09-01
dcterms.embargo.terms2013-09-01
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineChemistry
thesis.degree.grantorColorado State University
thesis.degree.levelMasters
thesis.degree.nameMaster of Science (M.S.)

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