[HTML][HTML] ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins

R Sarroukh, E Goormaghtigh, JM Ruysschaert… - … et Biophysica Acta (BBA …, 2013 - Elsevier
Amyloid refers to insoluble protein aggregates that are responsible for amyloid diseases but
are also implicated in important physiological functions (functional amyloids). The …

Cell-penetrating peptides: Promising therapeutics and drug-delivery systems for neurodegenerative diseases

M Pirhaghi, F Mamashli… - Molecular …, 2024 - ACS Publications
Currently, one of the most significant and rapidly growing unmet medical challenges is the
treatment of neurodegenerative diseases such as Alzheimer's disease (AD) and Parkinson's …

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

M Bucciantini, E Giannoni, F Chiti, F Baroni, L Formigli… - nature, 2002 - nature.com
A range of human degenerative conditions, including Alzheimer's disease, light-chain
amyloidosis and the spongiform encephalopathies, is associated with the deposition in …

Metastability of native proteins and the phenomenon of amyloid formation

AJ Baldwin, TPJ Knowles, GG Tartaglia… - Journal of the …, 2011 - ACS Publications
An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils
reveals that this structural form is likely to be the most stable one that protein molecules can …

FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils

G Zandomeneghi, MRH Krebs, MG McCammon… - Protein …, 2004 - Wiley Online Library
The presence of β‐sheets in the core of amyloid fibrils raised questions as to whether or not
β‐sheet‐containing proteins, such as transthyretin, are predisposed to form such fibrils …

Oligomeric intermediates in amyloid formation: structure determination and mechanisms of toxicity

M Fändrich - Journal of molecular biology, 2012 - Elsevier
Oligomeric intermediates are non-fibrillar polypeptide assemblies that occur during amyloid
fibril formation and that are thought to underlie the aetiology of amyloid diseases, such as …

Hydrophobic enhancement of dopa-mediated adhesion in a mussel foot protein

W Wei, J Yu, C Broomell, JN Israelachvili… - Journal of the …, 2013 - ACS Publications
Dopa (3, 4-dihydroxyphenylalanine) is recognized as a key chemical signature of mussel
adhesion and has been adopted into diverse synthetic polymer systems. Dopa's notorious …

Thermally induced fibrillar aggregation of hen egg white lysozyme

LN Arnaudov, R de Vries - Biophysical journal, 2005 - cell.com
We study the effect of pH and temperature on fibril formation from hen egg white lysozyme.
Fibril formation is promoted by low pH and temperatures close to the midpoint temperature …

Amyloid fibrils: Versatile biomaterials for cell adhesion and tissue engineering applications

S Das, RS Jacob, K Patel, N Singh, SK Maji - Biomacromolecules, 2018 - ACS Publications
Extracellular matrices (ECM) play an enormous role in any living system, controlling various
factors and eventually fates of cells. ECM regulates cell fate by providing constant …

Molecular recycling within amyloid fibrils

N Carulla, GL Caddy, DR Hall, J Zurdo, M Gairí, M Feliz… - Nature, 2005 - nature.com
Amyloid fibrils are thread-like protein aggregates with a core region formed from repetitive
arrays of β-sheets oriented parallel to the fibril axis,. Such structures were first recognized in …