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

MPG-Autoren

Pickhardt,  Marcus
external;
Neuronal Cytoskeleton and Alzheimer's Disease, Cooperations, Center of Advanced European Studies and Research (caesar), Max Planck Society;

Mandelkow,  Eckhard
external;
Neuronal Cytoskeleton and Alzheimer's Disease, Cooperations, Center of Advanced European Studies and Research (caesar), Max Planck Society;

Externe Ressourcen

https://onlinelibrary.wiley.com/doi/abs/10.1002/mabi.201700109
(Verlagsversion)

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Zitation

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.


Zitierlink: https://hdl.handle.net/21.11116/0000-0001-78D8-5
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.