Home > Publications database > Differently Selected D-Enantiomeric Peptides Act on Different A beta Species |
Journal Article | PreJuSER-9877 |
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2010
Liebert
Larchmont, NY
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Please use a persistent id in citations: doi:10.1089/rej.2009.0924
Abstract: Aging is the most significant risk factor for Alzheimer disease (AD). The pathological hallmark of AD is the accumulation of aggregated amyloid-beta (Abeta) forms and insoluble plaques, mainly composed of Abeta, in the brain of the patient. Recently, we reported on the selection of D-enantiomeric, Abeta-binding peptides D1 and D3. D1 was selected against aggregated Abeta species to address diagnosis by in vivo imaging of amyloid plaques, whereas D3 was selected using low-molecular-weight Abeta species, therefore addressing therapeutical studies. Here, we use a surface plasmon resonance method to confirm that both peptides show the desired binding specificities.
Keyword(s): Alzheimer Disease: diagnosis (MeSH) ; Alzheimer Disease: metabolism (MeSH) ; Alzheimer Disease: pathology (MeSH) ; Amyloid: analysis (MeSH) ; Amyloid: chemistry (MeSH) ; Amyloid beta-Peptides: chemistry (MeSH) ; Amyloid beta-Peptides: drug effects (MeSH) ; Amyloid beta-Peptides: metabolism (MeSH) ; Humans (MeSH) ; Oligopeptides: chemistry (MeSH) ; Oligopeptides: metabolism (MeSH) ; Oligopeptides: pharmacology (MeSH) ; Peptide Fragments: chemistry (MeSH) ; Peptide Fragments: isolation & purification (MeSH) ; Peptide Fragments: metabolism (MeSH) ; Peptide Fragments: pharmacology (MeSH) ; Plaque, Amyloid: chemistry (MeSH) ; Plaque, Amyloid: drug effects (MeSH) ; Plaque, Amyloid: metabolism (MeSH) ; Protein Binding (MeSH) ; Protein Isoforms: analysis (MeSH) ; Protein Isoforms: chemistry (MeSH) ; Protein Multimerization: drug effects (MeSH) ; Substrate Specificity (MeSH) ; Surface Plasmon Resonance (MeSH) ; Amyloid ; Amyloid beta-Peptides ; D3 peptide ; Oligopeptides ; Peptide Fragments ; Protein Isoforms ; J
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