ORGN 650 |
| Three different β-cyclodextrins, peracylated on the hydroxymethyl rim of the cyclodextrin ((6-Cn)-β-CD), and nine different nitrilotriacetic acid-modified guest ligands (R-NTA) have been prepared. These modular amphiphiles have been developed to promote crystallization of histidine-tagged proteins at the lipid-water interface via Ni(II)-NTA ligation. Pressure-area isotherm data suggest that the occupancy of the host sites within the (6-Cn)-β-CD monolayers vary as a function of the known host-guest binding constant for the unmodified β-CD host and R guest substituents. Negative-stain TEM shows that vesicles are formed upon sonication of (6-C10)-β-CD and (6-C16)-β-CD in 10 mM TRIS, pH 7.4 buffer. Exposure of (6-C16)-β-CD monolayers to Ne-adamantamide-lysine-NTA, Ni(II), and his6-GFP produced crystalline arrays of GFP that were more than 5 molecular layers thick. These results suggest that (6-Cn)-β-CD forms stable lyotropic phases that may be useful for templating the interfacial crystallization of histidine-tagged proteins or other molecules capable of interacting with the R-NTA guest ligands. |
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Proteins, Peptides, and Nucleotides
8:00 AM-11:00 AM, Wednesday, 16 March 2005 Convention Center -- Room 9, Oral
Division of Organic Chemistry |