Non-adhesive behavior of new nanostructured PNIPAM surfaces towards specific neurodegenerative proteins: application to storage and titration of Tau proteins

Macromol Biosci. 2012 Oct;12(10):1354-63. doi: 10.1002/mabi.201200116. Epub 2012 Aug 27.

Abstract

New nonfouling tubes are developed and their influence on the adhesion of neuroproteins is studied. The biomarkers are considered as single components (recombinant prion and Tau proteins) or in a solution of native and pathological forms. The samples are stored for 24 h at 4 °C in virgin and treated tubes layered with two different nanostructured coatings based on poly(N-isopropylacrylamide) with either a positive or a neutral charge, and the protein adhesion is monitored. The recombinant protein with a high pI is repelled from the nanostructured surface that has a negative ζ potential, whereas the recombinant protein with the lower pI is attracted. Furthermore, in the case of complex solutions, neutral nanostructured surfaces are able to retain all amyloid biomarkers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acrylamides / chemistry*
  • Acrylic Resins
  • Amyloid beta-Peptides / cerebrospinal fluid
  • Amyloid beta-Peptides / chemistry*
  • Coated Materials, Biocompatible / chemistry*
  • Enzyme-Linked Immunosorbent Assay
  • Humans
  • Nanostructures
  • Peptide Fragments / cerebrospinal fluid
  • Peptide Fragments / chemistry*
  • Photoelectron Spectroscopy
  • Polymers / chemistry*
  • Prions / cerebrospinal fluid
  • Prions / chemistry*
  • Protein Binding
  • Recombinant Proteins / chemistry
  • Solutions
  • Static Electricity
  • Surface Properties
  • Thermodynamics
  • tau Proteins / cerebrospinal fluid
  • tau Proteins / chemistry*

Substances

  • Acrylamides
  • Acrylic Resins
  • Amyloid beta-Peptides
  • Coated Materials, Biocompatible
  • Peptide Fragments
  • Polymers
  • Prions
  • Recombinant Proteins
  • Solutions
  • amyloid beta-protein (1-42)
  • tau Proteins
  • poly-N-isopropylacrylamide