ChiralCatLnCoils · De novo design of Lanthanide coiled coils for asymmetric catalysis

De novo design of Lanthanide coiled coils for asymmetric catalysis

Many biological activities are mediated by specific proteins or enzymes, which usually require metal ions for function. Enzyme-bound metal ions provide binding sites for the natural substrates and function as catalytic centers. This has motivated several attempts to reproduce, at least partially; the catalytic function of metalloenzymes, using metal bound coiled coil CC peptide complexes as models. The design and development of transition metal binding artificial peptides having specific chemical functions and/or interesting physical properties may offer exciting opportunities to advance modern science including medicine. However, this aim not only demands the ability to develop new protein structures capable of coordinating specific transition metal ions, but also requires insight into how their properties can be influenced by the interplay between coordination chemistry and the protein environment. In light of this dispute, a large majority of de novo (from first principles) Metallo Coiled coil (MCC) examples have focused their efforts on mimicking the active sites of native metalloproteins. Our overreaching objective was to develop de novo designed CC peptides, to generate miniature protein scaffolds with well-defined secondary, tertiary and quaternary structure, and with which structure-function relationships can more readily be established. Then we have investigated their metal binding (a range of bio & eco relevant transition metals and lanthanides) capability and interrogated their coordination chemistry, and attempted to use the MCC as catalysts, for which a real academic and industrial need exists.

Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз