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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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| Publicado no: | Biochem Biophys Rep |
|---|---|
| Main Authors: | , , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Elsevier
2016
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| Assuntos: | |
| Acesso em linha: | 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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