King's College London
Francis Crick Institute

Enzymes are the tools of nature. They are biological machines that facilitate reactions that are essential to life. For example, starch molecules in potatoes are too large to be absorbed, but enzymes break them down into smaller molecules allowing for absorption and this ultimately provides energy to the body. These systems work exceptionally well as they are able to control their motion, work in concert, and bind specific structures. Research on such systems has allowed us to not only understand their modes of action but also create useful applications. Over the past few decades, chemists have endeavored to mimic such systems using synthetic molecules and while great strides have been made these organic systems cannot match the specificity, complexity and directionality within biological processes. To create systems that function as enzymes, we must first take a step back and look at how they are made. Understanding synthetic systems is important to gain fundamental knowledge of how the tools work before moving to applications.

My research vision sets forward the development of a novel class of supramolecular hosts which will have the potential to understand and emulate tasks leveraged by enzymes for catalysis, built from the sequence polymers of life, i.e., foldamers. These unique cages will possess functionality that is observed in their biological counterparts such as compatibility. Inclusion of a light-activated molecular switch will allow for external control of the uptake and release of guest molecules. These systems will show unprecedented levels of control over the cavity, creating catalytic pockets, with the possibility to modify structures after the binding of specific biologically-relevant guests. These novel switchable supramolecular hosts will provide solutions to issues such as selectivity that chemists have struggled with bringing about potential untapped methods of drug delivery and treatment of diseases.