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Updated: Aug 21, 2026

Designing Silk-silk Protein Alloy Materials for Biomedical Applications
Published on: August 13, 2014
Metal-induced folding of a designed metalloprotein
Olesya A Kharenko1, Michael Y Ogawa
1Department of Chemistry, Center for Photochemical Sciences, Bowling Green State University, 141 Overman, Bowling Green, OH 43403, USA.
Abstract:
The metal-induced assembly of a designed peptide-based rubredoxin model is described. The C16C19-GGY peptide has the sequence Ac-K(IEALEGK)(2)(CEACEGK)(IEALEGK)GGY-amide in which the presence of the Cys-X-X-Cys metal binding domain of rubredoxin was used to place cysteine residues at the hydrophobic "a" and "d" positions upon formation of a homodimeric alpha-helical coiled-coil. Circular dichroism spectroscopy shows that the apopeptide exists as a random coil and assembles into a coiled-coil in the presence of Cd(2+). Metal binding is monitored by the appearance of a new LMCT band at 238 nm. UV-Vis titrations and SDS-PAGE experiments are used to show that this designed metalloprotein exists as a metal-bridged coiled-coil dimer.
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