Inhibition of cytotoxicity and amyloid fibril formation by a D-amino acid peptide that specifically binds to Alzheimer's disease amyloid peptide

Protein Engineering, Design and Selection

Volumn 21, Issue 4, 2008, Pages 241-246

  Wiesehan, K ^a   Stohr J ^b   Nagel Steger, L ^b   Van Groen, T ^c   Riesner, D ^b   Willbold, D ^a,b  

^a FORSCHUNGSZENTRUM JÜLICH   (Germany)

^b HEINRICH HEINE UNIVERSITY   (Germany)

^c UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

A ; Aggregation; Alzheimer's disease; Cytotoxicity; D amino acid peptide

Indexed keywords

AGGLOMERATION; AMINO ACIDS; CYTOTOXICITY; ELECTRON MICROSCOPY; FLUORESCENCE MICROSCOPY; PEPTIDES; POLYMERIZATION;

ALZHEIMER'S DISEASE; D-AMINO ACID PEPTIDE; POLYMER FORMATION;

DISEASES;

AMYLOID; DEXTRO AMINO ACID; THIOFLAVINE;

ALZHEIMER DISEASE; ANALYTIC METHOD; ANIMAL CELL; ARTICLE; CELL ASSAY; CONTROLLED STUDY; CYTOTOXICITY; ELECTRON MICROSCOPY; FLUORESCENCE; FLUORESCENCE CORRELATION SPECTROSCOPY; NONHUMAN; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; RAT;

AMYLOID BETA-PROTEIN; ANIMALS; CELL DEATH; CYTOTOXINS; MICROSCOPY, ELECTRON; PC12 CELLS; PEPTIDES; POLYMERS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RATS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; THIAZOLES;

EID: 41149162218     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzm054     Document Type: Article

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