Design of metastable β-sheet oligomers from natively unstructured peptide

M.J. Guerrero-Muñoz, D.L. Castillo-Carranza, U. Sengupta, M.A. White, R. Kayed

Producción científicarevisión exhaustiva

14 Citas (Scopus)


Amyloid oligomers represent the primary pathological species for neurodegenerative diseases such as Alzheimer's and Parkinson's diseases. Toxic oligomers are formed by many different proteins and peptides, but their polydispersity makes them highly dynamic and heterogeneous. One way to stabilize these structures is to prepare constrained peptides that can be used to study amyloid intermediates, to identify oligomer-specific drugs, and to generate conformational antibodies. These conformational antibodies have demonstrated that oligomers share a common epitope. In this research, we used a 40-amino acid unstructured segment of prion protein (Prp) 109-148 with substitutions of methionine for glycine (Prp-G) residues to prepare a stable and homogeneous population of β-sheet oligomer mimics. These structures were characterized by multiple biophysical and biochemical techniques that show characteristic features of oligomers. Finally, this preparation was not detected by three different sequence dependent prion antibodies.

Idioma originalEnglish
Páginas (desde-hasta)1520-1523
Número de páginas4
PublicaciónACS Chemical Neuroscience
EstadoPublished - 18 dic 2013
Publicado de forma externa

All Science Journal Classification (ASJC) codes

  • Bioquímica
  • Fisiología
  • Neurociencia cognitiva
  • Biología celular


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