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...

Descripción completa

Detalles Bibliográficos
Autores principales: Wall, Jonathan S., Williams, Angela, Wooliver, Craig, Martin, Emily B., Cheng, Xiaolin, Heidel, R. Eric, Kennel, Stephen J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5363963/
https://www.ncbi.nlm.nih.gov/pubmed/28345062
http://dx.doi.org/10.1016/j.bbrep.2016.08.007

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5363963/
https://www.ncbi.nlm.nih.gov/pubmed/28345062
http://dx.doi.org/10.1016/j.bbrep.2016.08.007

Ejemplares similares