Please use this identifier to cite or link to this item: http://dx.doi.org/10.25673/34683
Title: Modulation of amyloid peptides aggregation by hydrophilic polymers
Author(s): Evgrafova, ZhannaLook up in the Integrated Authority File of the German National Library
Referee(s): Binder, Wolfgang H.Look up in the Integrated Authority File of the German National Library
Schacher, FelixLook up in the Integrated Authority File of the German National Library
Granting Institution: Martin-Luther-Universität Halle-Wittenberg
Issue Date: 2020
Extent: 1 Online-Ressource (142 Seiten)
Type: HochschulschriftLook up in the Integrated Authority File of the German National Library
Type: Doctoral thesis
Exam Date: 2020-09-01
Language: English
URN: urn:nbn:de:gbv:3:4-1981185920-348781
Abstract: Die 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.
Fibrillogenesis 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.
URI: https://opendata.uni-halle.de//handle/1981185920/34878
http://dx.doi.org/10.25673/34683
Open Access: Open access publication
License: In Copyright
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