Measuring protein structure and stability of protein-nanoparticle systems with synchrotron radiation circular dichroism

Nano Lett. 2011 Oct 12;11(10):4480-4. doi: 10.1021/nl202909s. Epub 2011 Sep 28.

Abstract

We measure the structural and stability changes of proteins at nanomolar concentration upon interaction with nanoparticles. Using synchrotron radiation circular dichroism (SRCD), we measure a decrease of 6 °C in the thermal unfolding of human serum albumin upon interaction with silver nanoparticles while this does not happen with gold. The use of SRCD allows measuring critical parameters on protein-nanoparticle interactions, and it will provide experimental data on the relative stability of key biological proteins for nanotoxicology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Circular Dichroism*
  • Metal Nanoparticles*
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Static Electricity
  • Synchrotrons*

Substances

  • Proteins