Using bioinformatics methods, fragment KLVFFAQNVG (Аβ16-25) was found in the sequence of peptide Аβ1-42 responsible to its amyloidogenic properties. The fragment was chemically synthesized and obtained in sufficient amounts for studying the process of its amyloid formation. According to the electron microscopy data, under 5% DMSO and 50 мМ Tris-HCl, pH 7.5 this fragment forms morphology uncharacteristic of most amyloids. This morphology looks like wide flat ribbons/films up to 150 nm and higher. The morphology is of interest as bionanomaterial for adsorption of different biological objects from proteins and their complexes with proteins and nucleic acids to viral particles. Though the morphology of polymers formed by the Аβ16-25 fragment is unusual, according to X-ray diffraction data its preparations display the presence of two main reflections (4.6-4.8 Ǻ and 8-12 Ǻ) characteristic of cross-b structure of amyloid fibrils.
β1-42 peptide, amyloids, bionanomaterial, bioinformatics
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