New publication: "Towards standards for light scattering studies of proteins stability and nanoparticle-protein interactions".

Modulated 3D DLS results from Au NPs and BSA interaction. a) Cumulants results, b) CORENN results, were translational and rotational peak are distinguished, c) intensity ratio (rotation/translation) for the nanorods. 0.8 ml of Au NPs suspension, with C = 0.005 mg/ml, are mixed with 16 μl of BSA at C = 1.97 mg/ml.

Post publication date: 
Thursday, October 8, 2020

Protein-nanoparticle suspensions are nowadays widely studied for the development of medical and environmental biosensors. The complexity of interactions between nanoparticles and biological fluids, together with the increasing use of dynamic light scattering (DLS) for their characterization, support the need to develop common standards for DLS measurements and analysis, in order to enable a reliable comparison of measurement results.

In their study, the group of Prof. Schintke used LS Instruments patentened Modulated 3D DLS technology for the characterization of gold nanoparticles (Au NP), with spherical and rod shape, stabilized with sodium citrate, and their interaction with bovine serum albumin (BSA). Leveraging on the LS Instruments' unique CORENN DLS inversion algorithm they showed that for Au nanorods it is possible to distinguish the rotational and translational motion.

Moreover, they monitored the interaction of Au NPs and BSA over time, in order to analyze the first step of protein corona formation. Their results demonstrate that Au nanorods interact more than Au nanospheres with BSA. From the evolution of the rotational and translational peaks, they concluded that the proteins tend to bind on the long cylindrical side of the nanorods.

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