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dc.contributor.advisorŞeker, Urartu Özgür Şafak
dc.contributor.authorBeğli, Özge
dc.date.accessioned2019-09-18T08:03:58Z
dc.date.available2019-09-18T08:03:58Z
dc.date.copyright2019-09
dc.date.issued2019-09
dc.date.submitted2019-09-16
dc.identifier.urihttp://hdl.handle.net/11693/52447
dc.descriptionCataloged from PDF version of article.en_US
dc.descriptionThesis (M.S.): Bilkent University, Department of Materials Science and Nanotechnology, İhsan Doğramacı Bilkent University, 2019.en_US
dc.descriptionIncludes bibliographical references (leaves 91-97).en_US
dc.description.abstractNeurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease and Huntington’s disease are cognitively and physically debilitating and progressive diseases due to the gradual and irreversible loss of discrete neuronal populations in the brain. In addition to millions of people worldwide suffering from them, the prevalence of the neurodegenerative diseases dramatically increases with the increasing lifespan of the population. Most of the current therapeutic strategies either target toxic aggregates in neurons or support the healthy cells in diseased region. However, these interventions provide only symptomatic relief and deceleration of disease progression. Besides, aggregation involves a locking phase in which irreversible transition of soluble monomeric and oligomeric molecules into insoluble fibrous structures occurs. During aggregation, fragmentation of mature fibrils leads to the formation of new oligomeric structures possessing seeding activity. The seeds behaving as a nucleation unit trigger other structures to join the accumulated proteins. Synthetic biology is an emerging field that suggests therapeutic solutions for several diseases. Development of synthetic proteins such as artificial transcription factors and improved antibodies, artificial cell transplants with controlled secretion, designed inhibitory RNA molecules and antisense oligonucleotides, gene circuits and logic gates, synthetic viruses as an advanced delivery system and genome editing technologies using programmable nucleases are revolutionary approaches for the diagnosis and treatment of diseases. With the utilization of a variety of advanced tools, synthetic biology is extremely promising to treat neurodegenerative disorders too. In this study, biotechnological approaches and tools such as gene cloning, yeast surface display and phage display library have been used to target neurodegenerative proteins before aggregation takes place. Neurodegenerative proteins were cloned into a plasmid DNA within bacteria and displayed on the surface of Saccharomyces cerevisiae cells. A phage display library has been screened against those neurodegenerative proteins and binding peptides of these proteins have been selected following recursive rounds of binding and washing steps. Peptides that bind to neurodegenerative proteins with high affinity possess the potential to block them and prevent the initiation of aggregation. Beside to the promising results of neuroprotective and neurorestorative interventions, this strategy can provide prevention of aggregation which is the underlying cause of neurodegeneration.en_US
dc.description.statementofresponsibilityby Özge Beğlien_US
dc.format.extentxx, 133 leaves : illustrations (some color), charts (some color) ; 30 cm.en_US
dc.language.isoEnglishen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectNeurodegenerative diseasesen_US
dc.subjectSynthetic biologyen_US
dc.subjectAmyloiden_US
dc.subjectYeast surface displayen_US
dc.subjectPhage library displayen_US
dc.subjectProtein-ligand interactionsen_US
dc.titlePeptide based ligand discovery to prevent protein aggregation in neurodegenerative disease conditionsen_US
dc.title.alternativeNörodejeneratif hastalık koşullarında agregasyonu önlemek için peptit temelli ligand keşfien_US
dc.typeThesisen_US
dc.departmentInstitute of Materials Science and Nanotechnology UNAMen_US
dc.publisherBilkent Universityen_US
dc.description.degreeM.S.en_US
dc.identifier.itemidB122422
dc.embargo.release2020-03-13


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