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dc.contributor.authorZhang, Tong
dc.date.accessioned2018-06-05T04:30:14Z
dc.date.available2018-06-05T04:30:14Z
dc.date.issued2017-12
dc.identifier.otherzhang_tong_201712_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/zhang_tong_201712_ms
dc.identifier.urihttp://hdl.handle.net/10724/38084
dc.description.abstractThe cellular prion protein (PrP) is a glycosylphosphatidylinositol (GPI)-anchored plasma membrane protein, whose pathogenic isoform is a noxious inducer of numerous fatal neurodegenerative diseases. Sulfated glycosaminoglycans (GAGs), including heparin, are associated with prion proteins (PrP) misfolding and aggregation. However, the role of heparin in the PrP aggregation is less clear. Here, we investigate the PrP aggregation process through atomic force microscopy (AFM). Our result demonstrates heparin promotes protein aggregation by facilitating the formation of oligomers during the early nucleation stage. Full-length PrP binding to heparin is a two-step process that includes the formation of 1) short sporadic oligomers and 2) long stable fibrils. In addition, the force spectroscopy shows that interaction between PrP and heparin binding is mainly through electrostatic forces with an estimated Gibbs free energy of 28.53 kcal/mol.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectPrion proteins
dc.subjectHeparin
dc.subjectAFM
dc.subjectAggregation
dc.subjectOligomer
dc.subjectProtofibril
dc.subjectFibril
dc.titleThe Role of Heparin in the Prion Proteins Aggregation
dc.typeThesis
dc.description.degreeMS
dc.description.departmentChemistry
dc.description.majorChemistry
dc.description.advisorBingqian Xu
dc.description.committeeBingqian Xu
dc.description.committeeLianchun Wang
dc.description.committeeJason Locklin


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