COLL 232 |
| By combining nanografting and chemical activation of n-alkanethiols, AFM studies can provide new insight for in situ studies of protein–protein interactions with nanoscale resolution. First, two-dimensional arrays of nanopatterns are written with carboxylate headgroups using nanografting. The –COOH groups are then activated using EDC and NHS coupling chemistry. When protein solutions are introduced, the amine groups of lysine residues bond covalently to the nanopatterns forming a robust and stable linkage for sustained AFM imaging. The patterns are written within a methyl-terminated self-assembled monolayer, which resists the non-specific binding of proteins. Further biochemical reactions can be monitored in the AFM liquid cell by introducing proteins, antibodies or peptides to the protein nanopatterns. Studies with protein arrays of Staphylococcus protein A, ferritin and the beta subunit of the F1-ATP synthase protein will be presented. High resolution AFM images and height measurements provide information regarding binding and orientation of protein molecules.
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Fundamental Research in Colloid and Surface Chemistry
6:00 PM-8:00 PM, Monday, August 20, 2007 BCEC -- East Registration, Poster
Division of Colloid & Surface Chemistry |
