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Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives

Castelletto, V ; Ryumin, P ; Cramer, R ; Hamley, I W ; Taylor, M ; Allsop, D ; Reza, M ; Ruokolainen, J ; Arnold, T ; Hermida-Merino, D ; Garcia, C I ; Leal, M C ; Castaño, E

Scientific reports, 2017-03, Vol.7 (1), p.43637-43637, Article 43637 [Periódico revisado por pares]

England: Nature Publishing Group

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Título:
Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives
Autor: Castelletto, V ; Ryumin, P ; Cramer, R ; Hamley, I W ; Taylor, M ; Allsop, D ; Reza, M ; Ruokolainen, J ; Arnold, T ; Hermida-Merino, D ; Garcia, C I ; Leal, M C ; Castaño, E
Assuntos: Amino Acid Sequence ; Amyloid beta-Peptides - chemistry ; Amyloid beta-Peptides - metabolism ; Amyloid beta-Peptides - pharmacology ; Amyloidosis - drug therapy ; Amyloidosis - metabolism ; Amyloidosis - pathology ; Animals ; Cell Survival - drug effects ; Cytotoxicity ; Fibrils ; Grazing ; Hydrophobicity ; Ions ; Life Sciences ; Mass spectroscopy ; Molecular Structure ; Neuroblastoma ; Neuroblastoma cells ; Neurons - drug effects ; Neurons - metabolism ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; Peptides ; Protein Aggregates ; Protein Aggregation, Pathological - drug therapy ; Protein Aggregation, Pathological - metabolism ; Protein Structure, Secondary ; Rats ; Self-assembly ; Spectrometry, Mass, Electrospray Ionization ; Spectroscopy, Fourier Transform Infrared ; Toxicity ; X-Ray Diffraction ; X-ray scattering ; β-Amyloid
É parte de: Scientific reports, 2017-03, Vol.7 (1), p.43637-43637, Article 43637
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descrição: The self-assembly of two derivatives of KLVFF, a fragment Aβ(16-20) of the amyloid beta (Aβ) peptide, is investigated and recovery of viability of neuroblastoma cells exposed to Aβ (1-42) is observed at sub-stoichiometric peptide concentrations. Fluorescence assays show that NH -KLVFF-CONH undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac). In contrast, NH -K(Boc)LVFF-CONH undergoes hydrophobic collapse at a low concentration, followed by amyloid formation at a higher cac. These findings are supported by the β-sheet features observed by FTIR. Electrospray ionization mass spectrometry indicates that NH -K(Boc)LVFF-CONH forms a significant population of oligomeric species above the cac. Cryo-TEM, used together with SAXS to determine fibril dimensions, shows that the length and degree of twisting of peptide fibrils seem to be influenced by the net peptide charge. Grazing incidence X-ray scattering from thin peptide films shows features of β-sheet ordering for both peptides, along with evidence for lamellar ordering of NH -KLVFF-CONH . This work provides a comprehensive picture of the aggregation properties of these two KLVFF derivatives and shows their utility, in unaggregated form, in restoring the viability of neuroblastoma cells against Aβ-induced toxicity.
Editor: England: Nature Publishing Group
Idioma: Inglês

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Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives

Castelletto, V ; Ryumin, P ; Cramer, R ; Hamley, I W ; Taylor, M ; Allsop, D ; Reza, M ; Ruokolainen, J ; Arnold, T ; Hermida-Merino, D ; Garcia, C I ; Leal, M C ; Castaño, E

England: Nature Publishing Group

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