Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/34683
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dc.contributor.refereeBinder, Wolfgang H.-
dc.contributor.refereeSchacher, Felix-
dc.contributor.authorEvgrafova, Zhanna-
dc.date.accessioned2020-10-07T12:35:50Z-
dc.date.available2020-10-07T12:35:50Z-
dc.date.issued2020-
dc.identifier.urihttps://opendata.uni-halle.de//handle/1981185920/34878-
dc.identifier.urihttp://dx.doi.org/10.25673/34683-
dc.description.abstractDie Fibrillogenese des irreversibel aggregierenden Amyloid-β 1–40-Peptids (Aβ1–40) sowie des reversibel aggregierenden Nebenschilddrüsenpeptidhormon (PTH1-84) in Mischung oder in Konjugation mit hydrophilen thermoresponsiven Poly(oligo(ethylene glycol)m acrylaten) wird untersucht. Die Polymere werden mittels RAFT-Polymerisation synthetisiert, wodurch eine Serie von Polymeren mit unterschiedlichen Mn und einstellbarer Tcp herstellen werden konnten. Die Hydrophilie der Polymere wird durch die Anzahl der Ethylenglykoleinheiten in der Seitenkette, die Art der Endgruppe und des Polymerisationsgrades verändert. Die geeignete Kombination von hydrophoben Endgruppen mit hydrophilen Seitenketten steuert die Hydrophilie des Polymers und dadurch die Tcp des Polymers, die wiederum die Fibrillationswege der Peptide beeinflussen. Die Morphologie der erhaltenen Aggregate wird ebenfalls untersucht.ger
dc.description.abstractFibrillogenesis of the irreversibly aggregating amyloid-β 1–40 peptide (Aβ1–40) or reversibly aggregating parathyroid peptide hormone (PTH1-84) is investigated in a physical mixture or in covalent conjugation with hydrophilic thermoresponsive poly(oligo(ethylene glycol)m acrylates). The designed polymers are synthesized via RAFT-polymerization technique allowing us to prepare a series of polymers with different molecular masses and adjustable Tcp. The polymer's hydrophilicity is altered by variation of the number of ethylene glycol-units in the side chain, nature of the end group and the degree of polymerization of the polymers. The appropriate combination of hydrophobic end groups with hydrophilic side chains controls overall polymer's hydrophilicity and thus the polymer's Tcp, what in turn influences fibrillation pathways of the studied peptides in the presence of the polymers. The morphology of the obtained aggregates is also investigated.eng
dc.format.extent1 Online-Ressource (142 Seiten)-
dc.language.isoeng-
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/-
dc.subject.ddc540-
dc.titleModulation of amyloid peptides aggregation by hydrophilic polymerseng
dcterms.dateAccepted2020-09-01-
dcterms.typeHochschulschrift-
dc.typeDoctoral Thesis-
dc.identifier.urnurn:nbn:de:gbv:3:4-1981185920-348781-
local.versionTypepublishedVersion-
local.publisher.universityOrInstitutionMartin-Luther-Universität Halle-Wittenberg-
local.subject.keywordsAggregation, Amyloid β, Nebenschilddrüsenpeptidhormon, Kopplung, Fibrillen, Polymer-Peptid-Konjugate, Fibrillation, untere kritische Lösungstemperatur, thermoresponsive Polymere-
local.subject.keywordsaggregation, amyloid β, parathyroid hormone, conjugation, fibrils, polymer–peptide conjugates, fibrillation, lower critical solution temperature, thermoresponsive polymers-
local.openaccesstrue-
dc.identifier.ppn1734959479-
local.publication.countryXA-DE-
cbs.sru.importDate2020-10-07T12:33:38Z-
local.accessrights.dnbfree-
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