"Michael" Nanocarriers Mimicking Transient-Binding Disordered Proteins.

ABSTRACT

We report herein a very efficient synthesis strategy for the construction of artificial transient-binding protein-mimic nano-objects. Michael addition-mediated multidirectional self-assembly of individual polymeric chains at r.t. leads to "Michael" nanocarriers that in solution resemble disordered multidomain proteins, as revealed by a combination of small angle neutron scattering measurements and coarse-grained molecular dynamics simulation results, whereas in the dry state adopt a collapsed, globular morphology, as observed by transmission electron microscopy. This extended-to-compact morphology transition taking place upon solvent removal is of paramount importance, among other applications, for the construction of efficient biosensors based on immobilized protein-mimic nano-objects and for the development of transient vitamin-binding systems. As a proof of concept, we show the controlled delivery of vitamin B9 from these novel transient-binding nanocarriers.