Details

Autor(en) / Beteiligte

• Baldwin, Andrew J
• Bader, Reto
• Christodoulou, John
• MacPhee, Cait E
• Dobson, Christopher M
• Barker, Paul D

Titel

Cytochrome Display on Amyloid Fibrils

Ist Teil von

• Journal of the American Chemical Society, 2006-02, Vol.128 (7), p.2162-2163

Ort / Verlag

Washington, DC: American Chemical Society

Erscheinungsjahr

2006

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• Protein amyloid fibrils can be functionalized by coating the core protofilament with high concentrations of proteins and enzymes. This can be done elegantly by appending a functional domain to an amyloidogenic protein monomer, then assembling the monomers into a fibril. To display an array of biologically functional porphyrins on the surface of protein fibrils, we have fused the sequence of the small, soluble cytochrome b 562 to an SH3 dimer sequence that can form classical amyloid fibrils rapidly under well-defined conditions. The resulting fusion protein also forms amyloid fibrils and, in addition, binds metalloporphyrins, at half of the porphyrin binding sites as shown by UV−vis and NMR spectroscopies. Once metalloporphyrins are bound to the fibrils, the resulting holo-cytochrome domains are spectroscopically identical to the wild type cytochrome. The concentration of metalloporphyrins on a saturated fibril is estimated to be of the order of ∼20 mM, suggesting that they could be interesting systems for applications in nanotechnology.