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dc.contributor.authorWang, Yuxiao
dc.date.accessioned2015-05-07T04:30:11Z
dc.date.available2015-05-07T04:30:11Z
dc.date.issued2014-08
dc.identifier.otherwang_yuxiao_201408_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/wang_yuxiao_201408_ms
dc.identifier.urihttp://hdl.handle.net/10724/31335
dc.description.abstractA-kinase Anchoring Proteins (AKAPs) are key orchestrators that spatiotemporally regulate protein kinase A (PKA) activity by scaffolding pertinent intracellular proteins to form signaling complexes. Although PKA and AKAPs are involved in a variety of cellular and physiological functions, their exact roles in these functions and corresponding regulation mechanism are not well understood. In this thesis, several peptides mimicking the A-Kinase Binding (AKB) helix of AKAPs were chemically stabilized using all-hydrocarbon stapling, in order to target the docking/dimerization domain of PKA-R in an isoform-selective manner. The peptides are cell permeable in diverse human cell lines, highly isoform-selective for PKA-RI or –RII, and can effectively inhibit interactions between AKAPs and PKA-R in intact cells. Therefore, these peptides can be applied as valuable reagents in cell-based experiments to selectively disrupt AKAP-localized PKA-RI or -RII anchoring and aid in the study of compartmentalized type I or type II PKA signaling in cells.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectprotein kinase A
dc.subjectA-kinase anchoring protein
dc.subjectall-hydrocarbon staple
dc.subjectpeptide
dc.subjectfluorescence polarization
dc.subjectring-closing metathesis
dc.titleIsoform-selective disruption of AKAP-mediated PKA localization using hydrocarbon stapled peptides
dc.typeThesis
dc.description.degreeMS
dc.description.departmentPharmaceutical and Biomedical Sciences
dc.description.majorPharmacy
dc.description.advisorEileen Kennedy
dc.description.committeeEileen Kennedy
dc.description.committeeYujun Zheng
dc.description.committeeAnthony Capomacchia


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