Investigating fibrillar aggregates of Tau protein by atomic force microscopy

Methods Mol Biol. 2012:849:169-83. doi: 10.1007/978-1-61779-551-0_12.

Abstract

Atomic force microscopy (AFM) has been used in numerous studies to visualize and analyze the structure and conformation of biological samples, from single molecules to biopolymers to cells. The possibility to analyze native samples without fixation, staining and in physiological buffer conditions, combined with the sub-nanometer resolution, makes AFM a versatile tool for the analysis of protein aggregation and amyloid structures. Here, we describe the application of AFM to study fibrillar Tau protein aggregates.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adsorption
  • Aluminum Silicates / chemistry
  • Glutaral / chemistry
  • Humans
  • Microscopy, Atomic Force / methods*
  • Protein Multimerization*
  • Protein Structure, Secondary
  • Surface Properties
  • Time Factors
  • tau Proteins / chemistry*

Substances

  • Aluminum Silicates
  • tau Proteins
  • Glutaral
  • mica