Abstract

Applications in biomedicine, pharmaceutics, and diagnostics are driving interest in the specific coupling of de novo created recombinant protein polymers for the creation of precisely shaped nanomaterials. The genetic design of the protein polymers can be improved by using specially interacting peptides. The binding of specific proline-rich ligands by so-called WW-domains is an illustration of such an interaction. In this work, we looked at the production of these domains in the yeast Pichia pastoris as components of otherwise non-interacting protein polymers, as well as whether combining them would result in polymer coupling.