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 ha...

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Wedi'i Gadw mewn:
Manylion Llyfryddiaeth
Cyhoeddwyd yn:Biochem Biophys Rep
Prif Awduron: Wall, Jonathan S., Williams, Angela, Wooliver, Craig, Martin, Emily B., Cheng, Xiaolin, Heidel, R. Eric, Kennel, Stephen J.
Fformat: Artigo
Iaith:Inglês
Cyhoeddwyd: Elsevier 2016
Pynciau:
Research Article
Mynediad Ar-lein:https://ncbi.nlm.nih.gov/pmc/articles/PMC5363963/
https://ncbi.nlm.nih.gov/pubmed/28345062
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbrep.2016.08.007
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