Nanoparticles have been incorporated in many consumer products, however their safety and toxicity have not been clearly identified. This is made worse by difficulty in measuring how biological systems interact with nanoparticles.
Researchers from the Institute for Health and Consumer Protection (IHCP) and Diamond Light Source have used the Circular Dichroism beamline (B23) at Diamond to measure the alterations that proteins undergo when attaching to nanoparticles with unprecedented sensitivity. It is difficult to determine the structure and stability of the proteins bound to the nanoparticles, because of the nature of the solid/liquid interface and the low concentration of proteins. However B23 have developed a collimated microbeam feature which made this previously elusive measurement possible.
The research showed that when human serum albumin (the most abundant protein present in plasma) interacts with silver nanoparticles it is less stable than the free protein. On the contrary this destabilization does not happen when interacting with gold nanoparticles.
“This technique allows the measurement of critical parameters related to protein-nanoparticle interactions using only a few micrograms of proteins. It will provide much needed data on the relative stability of key biological proteins and aid in understanding and predicting the potential toxicology of nanomaterials and eventually may help in the design of the next generation of non toxic NP-based drug delivery systems.”
Luigi Calzolai from the Institute for Health and Consumer Protection (IHCP)
Measuring Protein Structure and Stability of Protein Nanoparticle Systems with Synchrotron Radiation Circular Dichroism, Nano Letters, (2011) 11 (10), pp 4480–4484 DOI: 10.1021/nl202909s
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