Nanoscale insights into full-length prion protein aggregation on model lipid membranes. Academic Article uri icon

Overview

abstract

  • The aggregates of the full-length human recombinant prion protein (PrP) (23-231) on model membranes were investigated by combining the atomic force microscopy (AFM) measurements and theoretical calculations at pH 5.0, showing the great effect of PrP concentration on its supramolecular assemblies on the lipid bilayer.

publication date

  • June 30, 2016

Research

keywords

  • Cell Membrane
  • Prion Proteins
  • Protein Aggregates

Identity

Scopus Document Identifier

  • 84977266778

Digital Object Identifier (DOI)

  • 10.1039/c6cc03029g

PubMed ID

  • 27284592

Additional Document Info

volume

  • 52

issue

  • 55