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Dr. Fiona Christie

Dr. Fiona Christie

Trainee Patent Attorney at HGF Limited – Intellectual Property Specialists

NanoDTC Student, Cohort 2009

Departments and Institutes


Key Publications

Research Overview

How Supramolecular Chemistry can control aggregation

The formation of clump-like  ordered structures in proteins has been associated with several diseases such as Alzheimer’s, Parkinson’s and type II diabetes, and is now thought to be a general feature of protein aggregation. There is considerable interest within the pharmaceutical industry in maintaining the integrity of protein-based drugs such as insulin during production and administration of the drug, however little is understood about the initial stages of aggregation.

My PhD is based on uncovering the supramolecular host-guest interactions between proteins or peptides, and special cucurbit[n]uril molecules. The cucurbit[n]uril family (written CB[n]) are a series of “barrel shaped” host molecules which are used to bind guest molecules, such as amino acids, to form larger constructs. The smaller “barrels” are capable of binding one guest while larger ones can accommodate up to two guests simultaneously. In this way, it is possible to “handcuff” molecules together in solution to harness or induce desired properties.

insulin molecule
Capturing insulin molecules using CB[8] can provide a way of interrupting the aggregation pathway of the protein, reducing the problems associated with delivery of insulin-based drugs. Shown in the figure are two insulin molecules thethered by one CB[8] molecule in the centre.
The focus of my research involves using the host-guest interactions of CB[7] and CB[8] to better understand the aggregation mechanism of human insulin. Current results indicate that on binding to the CB cavities, the natural aggregation pathway of insulin is interrupted and instead an immediate alternative aggregation pathway is observed. Under our protein denaturing conditions, the resulting aggregation process is temperature-dependent but yet remains fully reversible in the presence of CB[8]. On releasing the protein guest from the CB[8] host by increasing temperature, the insulin then aggregates irreversibly in a manner comparable to the native protein. We thus have a way to control aggregation by thermal incubation. From further studies, we hope to be able to control the aggregation of this protein during the storage and delivery processes to reduce the incidence of problematic insulin amyloid formation.

Fiona Christie

RSS Feed Latest news

Black researchers shaping the future

Oct 13, 2018

As the UK marks Black History Month, researchers from across the University talk about their route to Cambridge, their inspiration and their motivation.

‘Symposium as Sea’ in Antarctica

Oct 05, 2018

c2014 student Hannah Laeverenz Schlogelhofer has returned from an expedition to Antarctica as part of the Homeward Bound Leadership Programme.

NanoDTC Associates Programme

Sep 26, 2018

We are now accepting applications from current PhD students in Cambridge to become affiliated to the NanoDTC. Deadline 25th Oct.

Diversity Champ Carmen wins IoP Medal and Prize

Jul 11, 2018

Congratulations Carmen Palacios Berraquero (c2013) for winning the 2018 Jocelyn Bell Burnell Medal and Prize – an IoP award for outstanding early career female physicists