Analytical strategies for detecting nanoparticle-protein interactions.
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.
Li
Liwen
L
School of Chemistry and Chemical Engineering, Shandong University, Jinan, 250100, China.
Mu
Qingxin
Q
Zhang
Bin
B
Yan
Bing
B
D004586:Electrophoresis / Q000379:methods; D007700:Kinetics; D013058:Mass Spectrometry / Q000379:methods; D053758:Nanoparticles / Q000737:chemistry*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D013053:Spectrophotometry / Q000379:methods; D020349:Surface Plasmon Resonance / Q000379:methods
D011506:Proteins