Bioanalysis Rising Star Award finalist: Chris Williams
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Nominated by: Martijn Hilhorst, QPS (Groningen, The Netherlands)
Supporting comments:
“Chris joined the LC–MS/MS large molecule group 1 year ago as scientist/study director. I was impressed by his knowledge about peptide and protein chemistry. Although Chris’s knowledge and experience with mass spectrometry was limited, he quickly learned the tools of the trade and was quickly working at full speed in the LC–MS/MS lab. After a few weeks, he was working on complex LC–MS/MS projects involving antibody–drug conjugates, instable peptides as well as small molecule projects. He was invited to present his work on the EBF young scientist symposium. Next to the practical work, Chris also learned to fulfil the role as study director. This is a large accomplishment in this short period of time. Furthermore, and perhaps even more important, Chris has a very pleasant personality and a joy to work with. I strongly recommend him for the Rising Star Award, which will be most deserved.”
1Describe the main highlights of your bioanalytical work.
Although new to the field of bioanalysis, many publications from my time in academic research utilized assays that I developed from scratch, for the detailed analysis of peptides and proteins. For example, I developed methods for the expression and purification of large, multi-domain proteins for enzyme kinetic determination (Williams et al PNAS 2015) and protein complexes for biophysical/structural characterization (Groves et al BBRC 2017; Williams et al EMBO J 2012) as well as methods for the detection of post translationally modified proteins via immuno-capture (Williams et al JBC 2007; Danda et al 2017 Methods in Molecular Biology book series).
At QPS, I am responsible for the development of methods for the bioanalysis of peptides and proteins by LC–MS/MS. The main highlight of my work so far has been the development of two methods for a peptide that was extremely unstable in matrix. These studies required extensive method development work, to identify both conditions and additives to stabilize the peptide, including the development of a detailed sampling manual. Both methods have since been validated for regulated bioanalysis, a significant achievement.