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Inhibition of Amyloid β Protein Fibrillation by Polymeric Nanoparticles
Journal of the American Chemical Society, 2008 Copolymeric NiPAM:BAM nanoparticles of varying hydrophobicity were found to retard fibrillation of the Alzheimer's disease-associated amyloid beta protein (Abeta). We found that these nanoparticles affect mainly the nucleation step of Abeta fibrillation.
Sara Snogerup Linse +2 more
exaly +5 more sources
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Implications of excluded volume for chemical inhibition of protein fibrillation
Biochimica Et Biophysica Acta - General Subjects, 2020Two quantitative models for the effect of high total macromolecular volume occupancy ('macromolecular crowding') upon the chemical inhibition of protein fibrillation are presented. The first assumes that fibrillation is reversible, and the second assumes that fibrillation is irreversible.
Allen P Minton
exaly +3 more sources
Inhibiting ice recrystallization by amyloid protein fibrils
International Journal of Biological Macromolecules, 2023Ice recrystallization is harmful to the quality of frozen foods and the cryopreservation of cells and biological tissues, requiring biocompatible materials with ice recrystallization inhibition (IRI) activity. Emerging studies have associated IRI activity with amphiphilic structures.
Yuying, Fu +4 more
openaire +2 more sources
Inhibition of mitochondrial translocator protein prevents atrial fibrillation
European Journal of Pharmacology, 2010Atrial fibrillation is the most common arrhythmia encountered in clinical practice. It can cause severe complications such as congestive heart failure and stroke. However, identification of prime targets for efficient therapeutic intervention remains a challenge.
Yi-Han Chen, Zhuo Yu, Bing Jiang
exaly +3 more sources
Inhibition of Amyloid Peptide Fibrillation by Inorganic Nanoparticles: Functional Similarities with Proteins† [PDF]
Angewandte Chemie - International Edition, 2011 Aggregation of amyloid-β peptides (Aβ) into fibrils is the key pathological feature of many neurodegenerative disorders. Typical drugs inhibit Aβ fibrillation by binding to monomers in 1:1 ratio and display low efficacy. Here, we report that model CdTe nanoparticles (NPs) can efficiently prevent fibrillation of Aβ associating with 100–330 monomers at ...
Jeffrey Brender, Ming Yang, Seong Il Yoo
exaly +6 more sources
ACS Applied Materials & Interfaces, 2020
The abnormal folding and aggregation of amyloid-β protein (Aβ) is the main reason for the occurrence and development of Alzheimer's disease (AD). The discovery of novel inhibitors against Aβ aggregation is still the current research focus. Herein, we report the inhibitory effect of ulvan, an acidic polysaccharide from green algae of the genus Ulva ...
Fufeng Liu +8 more
openaire +2 more sources
The abnormal folding and aggregation of amyloid-β protein (Aβ) is the main reason for the occurrence and development of Alzheimer's disease (AD). The discovery of novel inhibitors against Aβ aggregation is still the current research focus. Herein, we report the inhibitory effect of ulvan, an acidic polysaccharide from green algae of the genus Ulva ...
Fufeng Liu +8 more
openaire +2 more sources
Research of the inhibition effects on the fibrillation of amyloid proteins
SCIENTIA SINICA Chimica, 2014This review summarized different kinds of inhibitors that affect the aggregation and fibrillation of amyloid proteins. The metal complexes were optimized as potential and effective inhibitors of amyloid proteins. Moreover, the interaction systems of amyloid proteins were also generalized in the aspect of thermodynamics studies.
WeiHong DU, XueSong WANG, BaoHuai WANG
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Brain Research, 2000
Amyloid beta-protein (Abeta) is present in soluble form in the plasma and cerebrospinal fluid (CSF) of normal people and patients with Alzheimer's disease (AD). However, in AD patients, Abeta gets fibrillized as the main constituent of amyloid plaques in the brain. Soluble synthetic Abeta also forms amyloid-like fibrils when it is allowed to age.
I, Ray +3 more
openaire +2 more sources
Amyloid beta-protein (Abeta) is present in soluble form in the plasma and cerebrospinal fluid (CSF) of normal people and patients with Alzheimer's disease (AD). However, in AD patients, Abeta gets fibrillized as the main constituent of amyloid plaques in the brain. Soluble synthetic Abeta also forms amyloid-like fibrils when it is allowed to age.
I, Ray +3 more
openaire +2 more sources
Current Alzheimer Research, 2004
Fibrillar amyloid beta-protein (Abeta) is the principal component of amyloid plaques in the brains of patients with Alzheimer's disease. We have studied the effect of walnut extract on Abeta fibrillization by Thioflavin T fluorescence spectroscopy and electron microscopy.
Neha, Chauhan +3 more
openaire +2 more sources
Fibrillar amyloid beta-protein (Abeta) is the principal component of amyloid plaques in the brains of patients with Alzheimer's disease. We have studied the effect of walnut extract on Abeta fibrillization by Thioflavin T fluorescence spectroscopy and electron microscopy.
Neha, Chauhan +3 more
openaire +2 more sources