Mapping interfacial chemistry induced variations in protein adsorption with scanning force microscopy.
In this work, we demonstrate the sensitivity of scanning force microscopy (SFM), operated in friction force mode, to adsorbed protein conformation or orientation. We employ patterned films of methyl- and carboxylate-terminated alkanethiolate monolayers on gold as substrates for protein adsorption to observe the effect of each functional group in the same image. Infrared spectroscopic and SFM studies of bovine fibrinogen (BFG) adsorption to single-component monolayers indicate that complete films of BFG that are stable to imaging are formed at each functional group. After adsorption of BFG to a patterned monolayer, we observe a contrast in friction images due to differences in adsorbed BFG conformation or orientation induced by each functional group. We also observe frictional contrast in films of other proteins adsorbed on patterned monolayers. These observations lead to the conclusion that SFM-measured friction is sensitive to adsorbed protein state.
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Department of Chemistry, University of Alberta, Edmonton, Canada.
McDermott
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D000327:Adsorption; D000818:Animals; D002417:Cattle; D005340:Fibrinogen / Q000737:chemistry; D018625:Microscopy, Atomic Force; D010449:Peptide Mapping / Q000379:methods; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared
D011506:Proteins; D005340:Fibrinogen