Atomic force microscopy to study molecular mechanisms of amyloid fibril formation and toxicity in Alzheimer's disease

E Drolle, F Hane, B Lee, Z Leonenko - Drug metabolism reviews, 2014 - Taylor & Francis
Alzheimer's disease (AD) is a devastating neurodegenerative disease characterized by
dementia and memory loss for which no cure or effective prevention is currently available …

Amyloid-β aggregation on model lipid membranes: An atomic force microscopy study

F Hane, E Drolle, R Gaikwad, E Faught… - Journal of …, 2011 - content.iospress.com
Amyloid fibril formation is generally associated with many neurodegenerative disorders,
including Alzheimer's disease (AD). Although fibril plaque formation is associated with …

[HTML][HTML] Changes in lipid membranes may trigger amyloid toxicity in Alzheimer's disease

E Drolle, A Negoda, K Hammond, E Pavlov… - PloS one, 2017 - journals.plos.org
Amyloid-beta peptides (Aβ), implicated in Alzheimer's disease (AD), interact with the cellular
membrane and induce amyloid toxicity. The composition of cellular membranes changes in …

Amyloid and membrane complexity: The toxic interplay revealed by AFM

C Canale, R Oropesa-Nuñez, A Diaspro… - Seminars in Cell & …, 2018 - Elsevier
Lipid membranes play a fundamental role in the pathological development of protein
misfolding diseases. Several pieces of evidence suggest that the lipid membrane could act …

Amyloid-forming proteins alter the local mechanical properties of lipid membranes

KA Burke, EA Yates, J Legleiter - Biochemistry, 2013 - ACS Publications
A diverse number of diseases, including Alzheimer's disease, Huntington's disease, and
type 2 diabetes, are characterized by the formation of fibrillar protein aggregates termed …

Alzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels

F Tofoleanu, NV Buchete - Prion, 2012 - Taylor & Francis
Fibrillar aggregates of misfolded amyloid proteins are involved in a variety of diseases such
as Alzheimer disease (AD), type 2 diabetes, Parkinson, Huntington and prion-related …

The two-fold aspect of the interplay of amyloidogenic proteins with lipid membranes

A Relini, O Cavalleri, R Rolandi, A Gliozzi - Chemistry and physics of lipids, 2009 - Elsevier
Investigating the pathways leading to the formation of amyloid protein aggregates and the
mechanism of their cytotoxicity is fundamental for a deeper understanding of a broad range …

[HTML][HTML] Amyloid-β oligomers have a profound detergent-like effect on lipid membrane bilayers, imaged by atomic force and electron microscopy

DC Bode, M Freeley, J Nield, M Palma… - Journal of biological …, 2019 - ASBMB
The ability of amyloid-β peptide (Aβ) to disrupt membrane integrity and cellular homeostasis
is believed to be central to Alzheimer's disease pathology. Aβ is reported to have various …

Membrane domain modulation of Aβ 1–42 oligomer interactions with supported lipid bilayers: an atomic force microscopy investigation

M Azouz, C Cullin, S Lecomte, M Lafleur - Nanoscale, 2019 - pubs.rsc.org
Alzheimer's disease is a devastating pathology affecting an increasing number of individuals
following the general rise in life expectancy. Amyloid peptide Aβ1–42 has been identified as …

Differences between amyloid-β aggregation in solution and on the membrane: insights into elucidation of the mechanistic details of Alzheimer's disease

SA Kotler, P Walsh, JR Brender… - Chemical Society …, 2014 - pubs.rsc.org
The association of the amyloid-β (Aβ) peptide with cellular membranes is hypothesized to be
the underlying phenomenon of neurotoxicity in Alzheimer's disease. Misfolding of proteins …