Polymers have been various biological applications, ranging from biocompatible scaffolds, to delivery vectors. Polymer bioconjugation, where a synthetic polymer is connected to an enzymatic or therapeutic protein has been shown to be particularly beneficial since the attached polymer can stabilize the protein against proteases, aggregation and immune responses. However, the connection between polymer structure and protein stability and activity is poorly understood. Using reversible deactivation radical polymerization, a wide library of polymer structures can be synthesized with flexibility over chemical functionality. Here we use two model enzymes, lysozyme from hen egg white, and cellulase from Fervidobacterium nodosum to study the impact of polymer structure on enzymatic activity and structural stability in functional polymer bioconjugates. In particular, polymers that have beneficial non-covalent attractions to substrates can dramatically enhance enzymatic activity, enabling polymer modification to be a new avenue for enzyme activation. Further, high molecular weight polymers and larger degrees of polymer modification can enhance protein structural stability.<br/>Synthetic polymers can also interact beneficially with lipids, creating optimized environments for studying membrane proteins. Membrane bound proteins represent 1/3 of all proteins, yet they represent only a small fraction of all known structures. Using well-defined copolymers of styrene and maleic acid enable well-defined nanoscale lipid discs to be created. In particular, the size of these discs can be varied by polymer composition, and they enable membrane protein encapsulation. This enables structural studies of these membrane proteins to be performed, and creates a versatile platform for structural biological studies.

Proteins and polymers: Synergies in bioconjugates and structures

255th National Meeting (2018)

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