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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)