Preparation of amyloid β‐protein for structural and functional studies

DB Teplow - Methods in enzymology, 2006 - Elsevier
Amyloid proteins cause a number of progressive, degenerative diseases. Among these is
Alzheimer's disease (AD), the etiology of which is linked to the formation of neurotoxic …

[HTML][HTML] Amyloid β interaction with model cell membranes–What are the toxicity-defining properties of amyloid β?

D Mrdenovic, IS Pieta, R Nowakowski, W Kutner… - International Journal of …, 2022 - Elsevier
Disruption of the neuronal membrane by toxic amyloid β oligomers is hypothesized to be the
major event associated with Alzheimer's disease's neurotoxicity. Misfolding of amyloid β is …

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

H LeVine III - Methods in enzymology, 1999 - Elsevier
Publisher Summary Despite the presence of a significant amount of carbohydrate in these
fibrils, the staining reaction was eventually shown to be because of the protein component …

Solution structure of the Alzheimer amyloid β‐peptide (1–42) in an apolar microenvironment: Similarity with a virus fusion domain

O Crescenzi, S Tomaselli, R Guerrini… - European journal of …, 2002 - Wiley Online Library
The major components of neuritic plaques found in Alzheimer disease (AD) are peptides
known as amyloid β‐peptides (Aβ), which derive from the proteolitic cleavage of the amyloid …

Synchrotron-based infrared and X-ray imaging shows focalized accumulation of Cu and Zn co-localized with β-amyloid deposits in Alzheimer's disease

LM Miller, Q Wang, TP Telivala, RJ Smith… - Journal of structural …, 2006 - Elsevier
Alzheimer's disease (AD) is characterized by the misfolding and plaque-like accumulation of
a naturally occurring peptide in the brain called amyloid beta (Aβ). Recently, this process …

Solution NMR studies of the Aβ (1− 40) and Aβ (1− 42) peptides establish that the Met35 oxidation state affects the mechanism of amyloid formation

L Hou, H Shao, Y Zhang, H Li, NK Menon… - Journal of the …, 2004 - ACS Publications
The pathogenesis of Alzheimer's disease is characterized by the aggregation and fibrillation
of the 40-residue Aβ (1− 40) and 42-residue Aβ (1− 42) peptides into amyloid plaques. The …

The α‐to‐β conformational transition of Alzheimer's Aβ‐(1–42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of …

S Tomaselli, V Esposito, P Vangone… - …, 2006 - Wiley Online Library
Current views of the role of β‐amyloid (Aβ) peptide fibrils range from regarding them as the
cause of Alzheimer's pathology to having a protective function. In the last few years, it has …

Insight into the kinetic of amyloid β (1–42) peptide self‐aggregation: elucidation of inhibitors' mechanism of action

M Bartolini, C Bertucci, ML Bolognesi, A Cavalli… - …, 2007 - Wiley Online Library
The initial transition of amyloid β (1–42)(Aβ42) soluble monomers/small oligomers from
unordered/α‐helix to a β‐sheet‐rich conformation represents a suitable target to design new …

Solution structures of micelle-bound amyloid β-(1-40) and β-(1-42) peptides of Alzheimer's disease

H Shao, S Jao, K Ma, MG Zagorski - Journal of molecular biology, 1999 - Elsevier
The amyloid β-peptide is the major protein constituent of neuritic plaques in Alzheimer's
disease. The β-peptide varies slightly in length and exists in two predominant forms:(1) the …

An improved method of preparing the amyloid β-protein for fibrillogenesis and neurotoxicity experiments

Y Fezoui, DM Hartley, JD Harper, R Khurana… - Amyloid, 2000 - Taylor & Francis
Synthetic amyloid β-protein (Aβ) is used widely to study fibril formation and the physiologic
effects of low molecular weight and fibrillar forms of the peptide on cells in culture or in …