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Single‐molecule imaging of protein adsorption mechanisms to surfaces
Author(s) -
Zareh Shan Kian,
Wang Yan Mei
Publication year - 2011
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/jemt.20954
Subject(s) - adsorption , streptavidin , protein adsorption , chemistry , molecule , deposition (geology) , chemical engineering , biophysics , kinetics , nanotechnology , materials science , biotin , organic chemistry , biochemistry , engineering , biology , physics , quantum mechanics , paleontology , sediment
Protein‐surface interactions cause the desirable effect of controlled protein adsorption onto biodevices as well as the undesirable effect of protein fouling. The key to controlling protein‐surface adsorptions is to identify and quantify the main adsorption mechanisms: adsorptions that occur (1) while depositing a protein solution onto dry surfaces and (2) after the deposition onto wet surfaces. Bulk measurements cannot reveal the dynamic protein adsorption pathways and thus cannot differentiate between the two adsorption mechanisms. We imaged the interactions of single streptavidin molecules with hydrophobic fused‐silica surfaces in real‐time. We observed both adsorbed proteins on surfaces and diffusing proteins near surfaces and analyzed their adsorption kinetics. Our analysis shows that the protein solution deposition process is the primary mechanism of streptavidin adsorption onto surfaces at the subnanomolar to nanomolar protein concentrations. Furthermore, we found that hydrophilic fused‐silica surfaces can prevent the adsorption of streptavidin molecules. Microsc. Res. Tech., 2011. © 2010 Wiley‐Liss, Inc.