Anchor peptide-mediated surface immobilization of a Grubbs-Hoveyda-type catalyst for ring-opening metathesis polymerization


Congratulations to Dr. Alexander R. Grimm and Dr. Daniel F. Sauer on their recent publication!

  Scheme of the project workflow, anchoring and polymerization with the Grubbs-Hoveyda anchor peptide construct Copyright: Bioconjugate Chem. A silica or (poly)propylene (PP) wafer (left) was coated with the Grubbs-Hoveyda type adhesion peptide construct (middle) and subsequently on the chip in neat substrate, polymerization was performed, yielding a hydrophobic layer.

In the new publication, catalytically active surfaces based on two different materials were generated. An organometallic Grubbs-Hoveyda type catalyst was attached to a variant of the anchor peptide LCI via maleimide cysteine conjugation. The Grubbs-Hoveyda type catalyst is able to perform olefin metathesis, a C=C double-bond rearrangement reaction that is not known to nature. With this protein-catalyst conjugate, ring-opening metathesis polymerization of a 7-oxanorbornene derivative in neat substrate was performed yielding a hydrophobic surface coverage, despite the starting surface was hydrophobic ((poly)propylene) or hydrophilic (silica). This immobilization strategy shows platform character and will allow to immobilize homogeneous catalyst on many types of surfaces to render them catalytically active. This work was realized in the division Next Generation Bioctalysts in cooperation with Professor Jun Okuda (Institute of Inorganic Chemisty, RWTH Aachen University) and it was possible through generous funding of the DFG and the BMBF. Generous samples of metal precursor by Umicore, Frankfurt, is gratefully acknowledged.

A. R. Grimm, D. F. Sauer, T. Mirzaei Garakani, K. Rübsam, T. Polen, M. D. Davari, F. Jakob, J. Schiffels, J. Okuda, U. Schwaneberg, Bioconjugate Chem. 2019, DOI: 10.1021/acs.bioconjchem.8b00874.