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4. Juni 2020

Modulation of amyloid β peptide aggregation by hydrophilic polymers.

Evgrafova, Z., et al. Physical Chemistry Chemical Physics 2019,21 (37), 20999-21006,DOI: http://dx.doi.org/10.1039/C9CP02683E.

A substantial number of diseases leading to loss of neurologic functions such as Morbus Alzheimer, Morbus Parkinson, or Chorea Huntington are related to the fibrillation of particular amyloidogenic peptides. We investigated amyloid-beta 1–40 peptide (Aβ1–40) fibrillation in mixture with thermoresponsive poly(oligo(ethylene glycol)macrylates), in which the polymer’s hydrophobicity is tuned by variation of the number of ethylene glycol-units in the side chain (m = 1–9), the end groups (B = butoxy; C = carboxy; D = dodecyl; P = pyridyldisulfide). The polymers were prepared via RAFT-polymerization. Less hydrophilic polymers (m = 1–2) were able to both decrease and elongate the lag (tlag) and characteristic times (tchar) of Aβ1–40 fibril formation in dependence of their end groups, molecular mass and hydrophilicity. Reproduced with permission from the PCCP Owner Societies.