Analytical strategies for detecting nanoparticle–protein interactions

Abstract

A significant increase in biomedical applications of nanomaterials and their potential toxicity demands versatile analytical techniques to determine protein–nanoparticle (NP) interactions. These diverse analytical techniques are reviewed. Spectroscopic methods play a significant role in studying binding affinity, binding ratio, and binding mechanisms. To elucidate NP–proteome interactions, chromatography and electrophoresis techniques are applied to separate NP-bound proteins and matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) to identify these proteins. Since NP–protein binding is a dynamic event, surface plasmon resonance (SPR) and quartz crystal microbalance (QCM) are methods of choice to study the kinetics of NP–protein binding.