Chris completed his undergraduate studies at the University of Oxford, graduating in 2005 with a first class MChem after a final year project with Prof. Paul Beer. After a year teaching physical and analytical chemistry at the University of Brighton, he returned to Paul Beer’s group for DPhil studies (co-funded and supervised by Johnson Matthey) which encompassed anion coordination, halogen bonding, crystallography, and metal nanoparticles. Chris was a finalist in the Reaxys PhD Prize, and was awarded EPSRC PhD+ funding for extension projects. In 2011 he moved to McGill University in Montreal as a Tomlinson, and then Banting Fellow in Prof. Hanadi Sleiman’s group, and worked at the interface of DNA, peptide, and polymer nanotechnologies. Chris returned to the UK in 2014, taking up a Marie Curie Experienced Researcher Fellowship in Prof. Ben Davis’s group at Oxford as part of an Innovative Training Network developing the use of filled carbon nanotubes in medicine and biology. Chris was appointed Lecturer in Chemistry at the University of Kent in July 2015 and is a member of the Functional Materials Group at the School of Physical Sciences.
You can see more about his research at his website https://research.kent.ac.uk/serpell/.
Room 309A, Ingram Building
Also view these in the Kent Academic Repository
You can see more about Dr Serpell's research at his website https://research.kent.ac.uk/serpell/.
Supramolecular chemistry is no longer just one field. Spurred by the 1987 Nobel Prize awarded to Cram, Lehn, and Pedersen, the non-covalent association of molecules has been studied widely and in many different forms. Small molecule methods include host-guest chemistry, molecular interpenetration, and crystal engineering, while macromolecular approaches encompass the association of amphiphilic polymers, and programmed assembly of DNA nanostructures and peptides into higher order structures. The most exciting advances are possible when these techniques are combined in an orthogonal fashion: there is a need to re-integrate the field to create truly novel functional materials rather than incremental steps. My research aims to interface these domains to generate nanostructures with unprecedented function.
The chemistry of life is dependent upon the supramolecular behaviour of specifically sequenced polymers: DNA stores the data that RNA communicates and translates, while proteins determine biological structure, signalling, and energetic pathways. Scientists have been ably exploiting DNA to create functional and precisely formed nanostructures for some years, and protein engineering is now moving from small modifications towards ‘peptide nanotechnology’. However, both of these assembly languages are limited by their lexicon of primarily natural monomers. Sequenced polymers comprised of an unlimited set of monomers could potentially harness all the self-assembly properties of the biopolymers while providing total freedom for the incorporation of functional or structural species taken from synthetic chemistry. Examples of sequenced polymers comprised of synthetic segments are currently sparse, but it has been shown that they are capable of forming highly novel systems such as catalytically active globular, single chain structures.
I have developed a strategy for the creation of non-natural sequence polymers by co-opting solid phase oligonucleotide synthesis through the use of short oligomers of well-known polymers in place of nucleosides. Control of the block length and order of the hydrophilic and hydrophobic units appended to DNA results in rationally altered supramolecular properties, determining whether random coil, assembled monomer, or micellar structures are formed. I am working to expand the library of monomers and develop understanding structure-function interplay for information storage molecular actuation, interface with biology, and light harvesting.
Access to large quantities of good quality water is one of the great challenges of our time. Although a range of water treatment technologies are available, each has its own advantages and drawbacks. In particular, desalination of sea water is still problematic. Reverse osmosis, the current favoured method, requires extremely high pressures. In contrast, water is purified in biological systems using only very minor pressure differences. The aquaporin family of transmembrane proteins provides the archetypal model for water transport: even protons cannot pass due to its unique supramolecular organisation of a water column within the channel.
Aquaporins themselves can be integrated into membranes for forward osmosis water treatment, but are unlikely to work under pressure in reverse osmosis which would be preferable from an engineering perspective. Additionally, the cost of producing significant quantities of aquaporin proteins may make scaleup impractical. I am designing and synthesising simplified artificial aquaporin mimics based upon the supramolecular features found in nature. Such systems are attractive in terms of stability under pressure, membrane loading density, and production cost.