The properties of holes in metallic film of subwavelength sizes have been an object of interrest for diffraction theory since
the 1940s and more recently experimentally studied[1]. Interresting transmissions effect has been observed, and is utilised
in scanning near-field microscopy.
I will propose a technique with promising applications in fabrication of holes in metallic film, using organic components.
This technique will use oxidizing peptides organised in a lattice on a Si-wafer, using fused SbsB-peptide complexes, which
will we used to cut the holes in the metallic films.
The selection of peptides will be done using commercially available phage display kits from New England Biolabs, employing an
engineered library of random peptides fused to the pIII proteine of M13. The phage will be tested for binding affinity to an
Ag substrate, and candidates will be selected and tested for oxidizing ability, using spectroscopy.
Peptides with appropriate oxidizing properties will then be fused to the N-terminus of SbsB[3] and self-assembled on an
Si-wafer. This self-assembled structure will have a regular lattice spacing.
Experimental
Selection of peptides:
An Ag substrate would be prepared as, outlined in the NEB PH.D12 manual, and several rounds of washing would be performed.
Elution of bound phage would be done by altering the pH. E. coli would be inoculated and candidates selected from the blue
plaques.
These candidates would be isolated and the peptides amplified.
Invidual peptides would be screened using a substrate and a solution of NO3 ions. Using absorbtion spectroscopy the solutions
would be monitored for changes towards a black colour.
Fusing to SbsB:
The newly identified peptide would be fused to the N-terminus of the SbsB protein, as this would enable it to self-assemble
on an Si-wafer as demonstrated by Moll et al[3].
The protein fusion would happen according to standard procedures of the pET system manual[4]. Fusion proteins would be
isolated according to published standard procedure [5].
Assembly on Si-substrate:
Self-assembly of the SbsB-peptide protein would be carried out as described in Moll et al [3].
For a wider spacing of oxidizing agents the fusion protein would be mixed in the phosphate buffer with regular SbsB in the
desired ratio.