Responsive Biopolymers: enzymatic control of assembly & disassembly

Lead Research Organisation: University of Leeds
Department Name: Institute of Membrane & Systems Biology

Abstract

Materials made with biological components have uses in medicine and beyond by virtue of the fact that simple small molecules spontaneously assemble to form more complicated structures. We have identified a type of molecule which assembles into large polymeric structures only after it is modified by an innocuous external factor. This provides exquisite control of the process of assembly, and will allow us to direct what is manufactured and where it is manufactured. A team of leading biologists will collaborate intimately with a team of leading polymer physicists to understand the theory of polymerisation of these materials, and to control the type of structure which can be built using derivatives of our initial small molecules.

Technical Summary

Biopolymers of nucleic acids and amino acids are proving to be highly versatile materials, which allow the fabrication of intricate structures by self-assembly for a variety of real world applications. To this point the vast majority of materials exhibit one dedicated behaviour (e.g. assembly into a given structure). Unlike these materials, we have identified a peptide which polymerises to form mats and fibres following enzymatic modification of the peptide (phosphorylation). This provides external control of polymerisation and depolymerisation which will allow one to direct the process of self-assembly. A discipline hop is proposed for the biochemist who invented this polymer to move to physics to develop a practical and theoretical understanding of peptide self assembly, and the control of order and form in the polymers created.

Publications

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