Protein binding for detection of small changes on a nanoparticle surface.
Protein adsorption on nanoparticles is closely associated with the physicochemical properties of particles, in particular, their surface properties. We synthesized two batches of polyacrylic acid-coated nanoparticles under almost identical conditions except for the heating duration and found differences in the head-group structure of the polyacrylic acid. The structure change was confirmed by NMR and MS. The two batches of particles had varied binding affinities to a selected group of proteins. Computational work confirmed that the head group of the polymer on the surface of a nanoparticle could directly interact with a protein, and small structural changes in the head group were sufficient to result in a significant difference in the free energy of binding. Our results demonstrate that protein adsorption is so sensitive to the surface properties of particles that it can reveal even small variations in the structure of a nanoparticle surface ligand, and should be useful for quick assessment of nanoparticle properties.
Department of Chemistry, University of California, Riverside, CA 92521, USA. chiaenc@ucr.edu wenwan.zhong@ucr.edu.
Shang
S
Zeng
Yu-ming M
YM
Huang
Chia-en A
CE
Chang
Wenwan
W
Zhong
D000180:Acrylic Resins / Q000737:chemistry / Q000378:metabolism*; D000327:Adsorption; D000818:Animals; D002147:Calmodulin / Q000378:metabolism*; D052203:Ferrosoferric Oxide / Q000737:chemistry*; D062105:Molecular Docking Simulation; D053758:Nanoparticles / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D013499:Surface Properties; D014981:Xenopus
D000180:Acrylic Resins; D002147:Calmodulin; C006903:carbopol 940; D052203:Ferrosoferric Oxide