Solvent effects on self-assembly of beta-amyloid peptide
نویسندگان
چکیده
منابع مشابه
Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives
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 NH2-KLVFF-CONH2 undergoes hydrophobic collapse and amyloid formation at the same critical aggregation concentration (cac)...
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ASKAROVA This work is licensed under a Creative Commons Attribution 3.0 United States License. Abstract Alzheimer's disease (AD) is a chronic neurodegenerative disorder, which is characterized by the accumulation of amyloid plaques and neurofibrillary tangles in specific regions of the brain, accompanied by impairment of the neurons, and progressive deterioration of cognition and memory of affe...
متن کاملProbing aromatic, hydrophobic, and steric effects on the self-assembly of an amyloid-β fragment peptide.
Aromatic amino acids have been shown to promote self-assembly of amyloid peptides, although the basis for this amyloid-inducing behavior is not understood. We adopted the amyloid-β 16-22 peptide (Aβ(16-22), Ac-KLVFFAE-NH(2)) as a model to study the role of aromatic amino acids in peptide self-assembly. Aβ(16-22) contains two consecutive Phe residues (19 and 20) in which Phe 19 side chains form ...
متن کاملAmyloid peptides incorporating a core sequence from the amyloid beta peptide and gamma amino acids: relating bioactivity to self-assembly.
A series of heptapeptides comprising the core sequence Aβ(16-20), KLVFF, of the amyloid β peptide coupled with paired N-terminal γ-amino acids are investigated in terms of cytotoxicity reduction and binding to the full Aβ peptide, both pointing to inhibition of fibrillisation for selected compounds. This is related to the self-assembly capacity of the heptapeptides.
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1995
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(95)79940-4