Friday, 04 February 2022 12:00

Presentation 1 (12h00-12h40) – Dr Sarah Hudson

Developing Challenging Molecules into Medicines: From Poorly Water Soluble Small Molecules to Peptides and Proteins

Presentation 2 (12h40-13h00) – Dr Stanislas Helle

Proteomics Analysis by Mass Spectrometry, Its Application in Plant Biology and Biopharmaceutical Research

ABSTRACT Presentation 1

It is well known that the drug discovery and development timeline is long, arduous and expensive. Many potential therapeutic molecules fail at the different stages of their development due to their challenging physicochemical properties, despite their biological activity against disease. At the Bernal Institute and in the SSPC Materials theme, the stability and the solution and solid-state properties of a range of therapeutic molecules with the goal of developing novel drug delivery strategies, formulations and analytical processes to expedite this development timeline are studied. Incorporating PAT technologies and pre-formulation strategies early in the development process reduces the attrition rate and decreases the overall cost and time it takes to get a drug to market. In this short presentation, the strategies developed which involve tailoring selected biomaterials to match the properties and target application of a range of therapeutic molecules, from poorly water soluble water molecules to peptides and proteins will be described.

ABSTRACT – Presentation 2

Mass spectrometry is nowadays the method of choice for the analysis of complex protein samples. It is used in every biological science domain, from plant biology to biopharmaceutical research. Among the existing methods, protein samples might be either separated in polyacrylamide gel prior to analysis or analysed directly without separation. Two main methods are described for the identification of proteins: bottom-up and top-down mass spectrometry. The bottom-up method consists of digesting proteins into peptide prior to analysis and identifying the proteins in the sample by matching the peptide sequences with known protein sequences available in databases. In top-down mass spectrometry, intact proteins are directly analysed and fragmented inside the mass spectrometer in order to identify the protein. Mass spectrometry proteomics also allow for quantification of proteins. This quantification can be realized label free, with the use of stable heavy isotope labelled standards or by labelling the peptides with isobaric mass tags. Here, some of these methods will be described which have been used for the quantification of proteins inside the potato starch granule, and which will be used for the upcoming analyses of IgG and Host Cell Proteins in the case of quality control for the purification of biopharmaceutical products

ABOUT THE PRESENTER

Dr Sarah Hudson studied chemistry at Trinity College Dublin, obtained a PhD from the University of Limerick in immobilised enzyme biocatalysis and did two postdoctoral positions in MIT, Boston and WIT, Waterford in drug delivery and pharmaceutics. Sarah is now a senior lecturer in chemistry in the Department of Chemical Sciences, a principal investigator in the SFI Research Centre for Pharmaceuticals (SSPC) and a researcher in the Bernal Institute, University of Limerick. Since graduating with her PhD in 2006, Sarah has secured over €8.5m in funding from EU, Exchequer and industrial funding with recent projects including a Disruptive Technologies Innovation Award (2019) and SFI New Frontiers funding (2020) which focus on the development of enzymes and peptides into medicines as well as leading a Marie Curie European Industrial Doctorate with TU Dortmond and Janssen in Belgium on the development of long acting injectable medicines (2019). These projects are based in the Bernal BioLabs and the SSPC. Sarah engages and supports industrial activities through close collaborations with many pharmaceutical companies in Ireland and Europe. She recently had a patent awarded on the development of nanomedicines and is currently looking at commercialisation of the invention, funded through an EI commercialisation award. Sarah has graduated 10 PhD and 2 Research Masters students, while her current team includes 23 researchers.

Dr Stanislas Helle is an SSPC post-doctoral researcher in protein characterisation at the Bernal Institute, University of Limerick. His work focuses on the analysis of biomolecules by mass spectrometry, more precisely on proteomics and metabolomics. Stanislas obtained his PhD in biochemistry in 2020. His PhD project involved proteomics analysis of potato starch granule. This project was a collaboration with the breeding company Florimond Desprez, in order to find out biomarkers for cold-induced sweetening of potato when tubers are kept at temperature below 5°C. On this same purpose, Stanislas continued to work with the University of Lille and Florimond Desprez as a research engineer for 1 year after his PhD on metabolomics of the potato tuber. His current task at the University of Limerick is to study the possibility of reusing the same protein A resin for the purification of multiple products, by analysing the column eluate using mass spectrometry. This project is a partnership with several biopharmaceutical industries, namely, Pfizer, Eli Lilly, MSD, Janssen, BMS.

For further information, please contact: edmond.magner@ul.ie