Dendrimers reduce toxicity of Aβ 1-28 peptide during aggregation and accelerate fibril formation

Nanomedicine: Nanotechnology, Biology, and Medicine

Volumn 8, Issue 8, 2012, Pages 1372-1378

  Klajnert, Barbara ^a   Wasiak, Tomasz ^a   Ionov, Maksim ^a   Fernandez Villamarin, Marcos ^b   Sousa Herves, Ana ^b   Correa, Juan ^b   Riguera, Ricardo ^b   Fernandez Megia, Eduardo ^b  

^a UNIVERSITY OF LODZ   (Poland)

^b s n   (Spain)

Author keywords

A 1 28; Alzheimer's disease; Amyloid peptide; Dendrimer

Indexed keywords

AGGREGATION PROCESS; ALZHEIMER'S; ALZHEIMER'S DISEASE; AMYLOID FIBRIL; AMYLOID PEPTIDES; CD SPECTRA; FIBRIL FORMATION; MORPHOLINES;

AGGLOMERATION; DENDRIMERS; GLYCOLS; GLYCOPROTEINS; TOXICITY; TRANSMISSION ELECTRON MICROSCOPY;

PEPTIDES;

AMYLOID BETA PROTEIN[1-40]; DENDRIMER; GALLIC ACID DERIVATIVE; GALLIC ACID TRIETYLENE GLYCOL; TRIETHYLENE GLYCOL; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; CHEMICAL STRUCTURE; CONTROLLED STUDY; CYTOTOXICITY; FIBER; HAMSTER; NONHUMAN; PROTEIN AGGREGATION; TRANSMISSION ELECTRON MICROSCOPY;

ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; ANIMALS; CELL LINE; CELL SURVIVAL; CRICETINAE; CRICETULUS; DENDRIMERS; FIBROBLASTS; GALLIC ACID; MICROSCOPY, ELECTRON, TRANSMISSION; PEPTIDE FRAGMENTS; POLYETHYLENE GLYCOLS;

EID: 84867892719     PISSN: 15499634     EISSN: 15499642     Source Type: Journal    
DOI: 10.1016/j.nano.2012.03.005     Document Type: Article

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