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

DOI: 10.1021/nl202909s DOI Help
PMID: 21932791 PMID Help

Authors: Stefania Laera (European Commission, Joint Research Centre, Institute for Health and Consumer Protection) , Giacomo Ceccone (European Commission, Joint Research Centre, Institute for Health and Consumer Protection) , Francois Rossi (European Commission, Joint Research Centre, Institute for Health and Consumer Protection) , Douglas Gilliland (European Commission, Joint Research Centre, Institute for Health and Consumer Protection) , Rohanah Hussain (Diamond Light Source) , Guiliano Siligardi (Diamond Light Source) , Luigi Calzolai (European Commission, Joint Research Centre, Institute for Health and Consumer Protection)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nano Letters , VOL 11 (10) , PAGES 4480 - 4484

State: Published (Approved)
Published: October 2011
Diamond Proposal Number(s): 6192

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.

Journal Keywords: Protein-nanoparticle interaction; protein structure; protein stability; circular dichroism; synchrotron radiation

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


Instruments: B23-Circular Dichroism

Added On: 13/10/2011 15:21

Discipline Tags:

Drug Delivery Health & Wellbeing Materials Science Nanoscience/Nanotechnology Biophysics Life Sciences & Biotech

Technical Tags:

Spectroscopy Circular Dichroism (CD)