A novel method for quantifying peripheral tissue amyloid load by using the radiolabeled amyloidophilic peptide, p5
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چکیده
منابع مشابه
Secondary structure propensity and chirality of the amyloidophilic peptide p5 and its analogues impacts ligand binding - In vitro characterization
BACKGROUND Polybasic helical peptides, such as peptide p5, bind human amyloid extracts and synthetic amyloid fibrils. When radiolabeled, peptide p5 has been shown to specifically bind amyloid in vivo thereby allowing imaging of the disease. Structural requirements for heparin and amyloid binding have been studied using analogs of p5 that modify helicity and chirality. METHODS Peptide-ligand i...
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ژورنال
عنوان ژورنال: Amyloid
سال: 2013
ISSN: 1350-6129,1744-2818
DOI: 10.3109/13506129.2012.757216