Repetitive-Selection Synthesis of Surface Bound Metal Binding Proteins.
Abstract
A silica surface is reacted with a tridentate siloxane to introduce appropriately spaced tris-aminoalkyl (aryl) groups as a template for protein assembly. The modified surface was reacted with simple aldehyde-modified amino acid derivatives. Only bipyridine-containing aldehyde was reacted with the surface in the presence of Fe(II) ion whereas no selective binding was observed in the absence of metal ions. The selection experiments with these simple aldehyde-modified amino acid derivatives demonstrate the feasibility of the repetitive-selection cycle to assemble a specific metal binding site on silica surface. A three-helix bundle protein was synthesized in solution to test structural stability. The resulting protein was found to be highly helical as expected. The protein, however, appears to be a molten globule instead of a native-like folded state.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 11, 1996
- Accession Number
- ADA314319
Entities
People
- Tomikazu Sasaki
Organizations
- University of Washington