Artificial proteins could be closer to participating in natural biochemical pathways after UK and US researchers show that bacteria will process amino acid sequences entirely unrelated to any natural protein to produce a fully functioning cytochrome.
The burgeoning field of synthetic biology demands that functional artificial proteins and enzymes seamlessly integrate with natural proteins and substrates. ‘We’re trying to build artificial proteins that exhibit some of the properties and chemistries of natural proteins,’ explains team member Ross Anderson from the University of Bristol.
Anderson and colleagues have used a relatively new methodology called the maquette approach that lets them escape some of the complexities of natural systems to construct their artificial cytochrome. They begin with a generic protein sequence designed only to fold into a 4-helix bundle. Engineered elements are added onto the stripped-down protein chassis; the role of every residue in the amino acid sequence is defined and adjusted by altering critical residues.
Read the full article in Chemistry World»
Read the original journal article online:
Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette
J. L. Ross Anderson, Craig T. Armstrong, Goutham Kodali, Bruce R. Lichtenstein, Daniel W. Watkins, Joshua A. Mancini, Aimee L. Boyle, Tammer A. Farid, Matthew P Crump, Christopher C. Moser and P. Leslie Dutton
Chem. Sci., 2014, Advance Article, DOI: 10.1039/C3SC52019F