ZiCo: a peptide designed to switch folded state upon binding zinc.
We describe a novel approach to the design of a metal-triggered conformational switch. Specifically, two distinct protein-folding motifs were merged into one polypeptide sequence. The target structures were an alpha-helical coiled-coil trimer and zinc-bound monomer. Solution-phase spectroscopic, sedimentation, and binding studies confirmed the key aspects of the design. Both forms of the peptide were cooperatively folded, and the switch between them was reversible. This design process potentially presents a novel route to peptide-based biosensors.
Cerasoli
Eleonora
E
Department of Biochemistry, School of Life Sciences, University of Sussex, Falmer BN1 9QG, UK.
Sharpe
Belinda K
BK
Woolfson
Derek N
DN
D001665:Binding Sites; D002712:Chlorides / Q000737:chemistry* / Q000378:metabolism; D002942:Circular Dichroism; D004492:Edetic Acid / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared; D013696:Temperature; D015032:Zinc / Q000737:chemistry* / Q000378:metabolism; D017967:Zinc Compounds / Q000737:chemistry* / Q000378:metabolism
D002712:Chlorides; D010455:Peptides; D017967:Zinc Compounds; C016837:zinc chloride; D004492:Edetic Acid; D015032:Zinc