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  Gaining insights into specific drug formulation additives for solubilizing a potential Anti-Alzheimer disease drug B4A1

Lawatscheck, C., Pickhardt, M., Grafl, A., Linkert, K., Polster, F., Mandelkow, E., et al. (2017). Gaining insights into specific drug formulation additives for solubilizing a potential Anti-Alzheimer disease drug B4A1. Macromolecular Bioscience, 17(10, S1): 1700109. doi:10.1002/mabi.201700109.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-0001-78D8-5 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0007-50D9-A
Genre: Zeitschriftenartikel

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https://onlinelibrary.wiley.com/doi/abs/10.1002/mabi.201700109 (Verlagsversion)
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Free Access (= Open Access?)
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Urheber

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 Urheber:
Lawatscheck, Carmen1, Autor
Pickhardt, Marcus1, 2, Autor
Grafl, Anna1, Autor
Linkert, Katharina1, Autor
Polster, Frank1, Autor
Mandelkow, Eckhard1, 2, Autor
Boerner, Hans G.1, Autor
Affiliations:
1external, ou_persistent22              
2Neuronal Cytoskeleton and Alzheimer's Disease, Cooperations, Center of Advanced European Studies and Research (caesar), Max Planck Society, Ludwig-Erhard-Allee 2, 53175 Bonn, DE, ou_2173677              

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Schlagwörter: -
 Zusammenfassung: The pharmacological profiles of small molecule drugs are often challenged by their poor water solubility. Sequence-defined peptides attached to poly(ethylene glycol) (PEG) offer opportunities to overcome these difficulties by acting as drug-specific formulation additives. The peptide-PEG conjugates enable specific, noncovalent drug binding via tailored peptide/drug interactions as well as provide water solubility and drug shielding by well-solvated PEG-blocks. A systematic set of specific solubilizers for B4A1 as a potential anti-Alzheimer disease drug is synthesized and variations involve the length of the PEG-blocks as well as the sequences of the peptidic drug-binding domain. The solubilizer/B4A1 complexes are studied in order to understand contributions of both PEG and peptide segments on drug payload capacities, drug/carrier aggregate sizes, and influences on inhibition of the Tau-protein aggregation in an in vitro assay.

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 Datum: 2017-05-102017-10
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000412816700018
DOI: 10.1002/mabi.201700109
 Art des Abschluß: -

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Quelle 1

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Titel: Macromolecular Bioscience
  Kurztitel : Macromol Biosci.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Weinheim : Wiley-VCH Verlag GmbH
Seiten: - Band / Heft: 17 (10, S1) Artikelnummer: 1700109 Start- / Endseite: - Identifikator: ISSN: 1616-5187
CoNE: https://pure.mpg.de/cone/journals/resource/954925586298_1