A triangular molecular tile, composed of peptides for the sides and a designed amino acid for each corner, will be utilized to prepare a self-assembled monolayer on gold. The rigid corner amino acid, amino methyl benzoyl benzoic acid (AMBBA) will be used as a template to impart the triangular structure to the molecule by keeping the peptides from collapsing on each other. The molecular tile will self-assemble due to the covalent bonds formed between the cysteines' thiols and the gold surface. A patterned nanoscale assembly of tiles is expected due to the formation of beta sheets between peptide sides of adjacent tiles. The side of the triangle or precursor peptide will first be assembled on gold and examined with ESCA in order to determine whether both cysteines are forming covalent bonds with the surface. NEXAFS will be usedto determine the orientation of the peptide. The AMBBA will further be examined to determine if its benzophenone-type properties will be a ble to tet her proteins when activated with the proper wavelength of light. Nitrogen content will also be followed by ESCA. An increase in nitrogen would indicate that the proteins have been tethered. Protein activity will be determined with a fluorogenic substrate. Chymotrypsin will be used as the first protein but since the mode of tethering is not protein specific, any protein could be utilized. The sequence of the peptide could also be varied in order to induce protein attraction and perhaps protein orientation.
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