Nucleoporins are the family of proteins responsible for selective transport of biomolecules into and out of the nucleus, forming gel-filled pores in the nuclear membrane that control transport and protect the cell’s genetic cargo.  These proteins show a remarkable ability to selectively filter just a small fraction of proteins into the nucleus with high flux, and this is believed to be based on dynamic bonding in a network-like structure.  Recently, we have shown that the transport function of the nuclear pore can be replicated with a minimal consensus repeat sequence derived from nucleoporins, yielding nucleoporin-like proteins (NLPs).  These NLPs enable fundamental research into how the structure of the consensus repeat affects its properties.  Through a series of rational mutations, we have prepared a small library of different NLP derivatives specifically mutated to understand the effect of different regions of the consensus repeat.  Biophysical characterization enables us to understand how changes in sequence affect binding and interaction in the materials.<br/> <br/>To provide a more fundamental understanding of possible separation mechanisms, we have used the concepts of associative polymer diffusion to put forward a hypothesis to explain the function of these simplified NLPs based on the presence of walking and hopping diffusive modes in the gels.  This hypothesis suggests design rules which allow the same transport properties observed in NLPs to be replicated in peptide-functionalized poly(ethylene glycol) (PEG) gels, completing the design cycle of adapting the performance of a natural material to a fully synthetic system based on insight into its fundamental transport mechanism. <br/>

Dynamic bonding in nucleoporin-like protein materials

255th National Meeting (2018)

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