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Terahertz Applications Group

Department of Chemical Engineering and Biotechnology
 

In collaboration with MedImmune, the EPSRC Centre for Doctoral Training in Sensor Technologies and Applications is inviting applications for a fully funded 1+3 years MRes + PhD studentship commencing in October 2017. More information about the programme can be found on http://cdt.sensors.cam.ac.uk/.

The pharmaceutical industry is increasingly turning to complex mixtures for their formulations in order to increase stability, efficacy, and bioavailability. 

Recent advances have highlighted that protein-sugar dispersions are a potential new route for advanced dosage forms. Yet such designs suffer from the same preparative issues that most new formulations have, that is understanding how to efficiently manufacture the product to maximise stability and efficacy. But unlike their small-molecule (and often mono-disperse) counterparts, such mixtures are difficult to analyse in situ because of the complexity of the interactions present.

Terahertz time-domain spectroscopy (THz-TDS) is a powerful tool for the non-destructive extraction of important parameters from solid materials, such as amorphous stability, molecular mobility, and intermolecular interaction strengths. It is a valuable technique for the characterisation of amorphous stability via the measurement of the strength of the intramolecular relaxation process, which can be directly linked to the stability of amorphous mixtures. Additionally, recent studies have used THz-TDS to obtain detailed mechanical (elastic) data of a crystalline polypeptide, highlighting the ability to understand how certain interactions lead to bulk mechanical properties. Such analyses are critical for understanding the dynamics of pharmaceutical mixtures, since a complete picture regarding the molecular arrangements can have profound implications for drug formulation and delivery, i.e. how to best manufacture and store the material.

This project aims to extend the utility of THz-TDS for the characterisation of protein-drug mixtures, in order to better understand how protein structure, specifically secondary structure, affects the solid-state dynamics and bulk properties.

For further details and to apply please visit (Closing date 28 February 2017).