Structure and stability of proteins interacting with nanoparticles

DOI: 10.1021/bk-2012-1120.ch038

Authors: Luigi Calzolai (IHCP-JRC) , Stefania Laera (European Commission -Joint Research Centre) , Giacomo Ceccone (Joint Research Centre Institute for Health and Consumer Protection) , Francois Rossi (European Commission -Joint Research Centre)
Co-authored by industrial partner: No

Type: Book Chapter

State: Published (Approved)
Published: December 2012
Diamond Proposal Number(s): 7993 , 7505

Abstract: The behavior and toxicological properties of nanoparticles (NP) in biological medium depends heavily on their interactions with proteins. In return, the structure, stability and biological properties of the proteins that interact with the nanoparticles are strongly affected by this interaction. Unfortunately, the mechanisms of interaction and their structural consequences are very difficult to analyse. Here we show the use of advanced biophysical techniques to obtain information on the structure and stability of protein-nanoparticle complexes. By using circular dichroism spectroscopy it is possible to detect changes in the secondary structure and stability of proteins upon interaction with nanoparticles. Moreover, by using nuclear magnetic resonance experiments, it is even possible to detect the specific domain of proteins interacting with nanoparticles.

Journal Keywords: Nanoparticle; Circular Dichroism; Proteins; Toxicology

Subject Areas: Biology and Bio-materials, Chemistry, Materials


Instruments: B23-Circular Dichroism

Other Facilities: No

Added On: 25/03/2013 16:38

Discipline Tags:

Biochemistry Chemistry Materials Science Nanoscience/Nanotechnology Life Sciences & Biotech

Technical Tags:

Spectroscopy Circular Dichroism (CD)