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Updated: Feb 2, 2026

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
Published on: April 28, 2022
Structural analysis of the Aβ(15-40) amyloid fibril based on hydrophobicity distribution
Dawid Dułak1, Mateusz Banach2, Malgorzata Gadzała3
1ABB Business Services Sp. z o.o., Żegańska 1, 04-713 Warszawa, Poland.
Abstract:
The Aβ42 amyloid is the causative factor behind various neurodegenerative processes. It forms elongated fibrils which cause structural devastation in brain tissue. The structure of an amyloid seems to be a contradiction of protein folding principles. Our work focuses on the Aβ(15-40) amyloid containing the D23N mutation (also known as the "Iowa mutation"), upon which an in silico experiment is based. Models generated using I-Tasser software as well as the fuzzy oil drop model - regarded as alternatives to the amyloid conformation - are compared in terms of their respective distributions of hydrophobicity (i.e. the existence of a hydrophobic core). In this process, fuzzy oil drop model parameters are applied in assessing the propensity of selected fragments for undergoing amyloid transformation.
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