2014 Young Investigator: Laura Cole

Bioanalysis rising star award
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Laura Cole

 

Nominee:

Nominated By: 

 

Supporting Comments:

What made you choose a career in bioanalysis?

For me, bioanalysis represents the merger of my two favorite science disciplines; biology and chemistry. Prior to completing my PhD I obtained an honors degree in Biomedical Sciences (BSc Hons). I chose elective modules which reflected my interest in biochemistry with an analytical science focus. I decided to develop this interest further by choosing a  work placement in this area and completing a  final year research project in Analytical Science entitled ‘Development of HPLC techniques for the analysis of antimicrobial peptides in scorpion haemolymph’. All of my previous bioanalysis work has fed my interest in the merger of analytical science and biological systems.

Describe the main highlights of your bioanalytical research, and its importance to the bioanalytical community.

I have contributed to MS imaging development through the analysis of drug treatment time course studies, the introduction of a multi-peptide recombinant standard as an imaging tool and, more recently, MS imaging and conventional proteomics to validate treatment response post administration of a vascular disrupting agent.

Cole et al., (2011) included MALDI profiling and imaging of gross pharmacological responses in tumour tissue post administration of vascular disrupting agent ‘Fosbretabulin’ and included multivariate statistics to assess protein induction. Ion mobility separation (IMS) has played a key role in my publication outputs and Cole et al., (2013) described a novel ‘IMS TAG’ imaging tool which comprised of an artificial multi-peptide recombinant construct. This was used as a means of validation in MALDI-IMS imaging, employing visualization of the digested recombinant construct and further validation via assessment of the drift time of corresponding product ions. My most recent publication outputs have been a paper and an Ebook chapter, accepted in December 2013. My most recent publication (Cole et al., 2014), accepted by ‘Proteomics’ incorporates label free quantitative MALDI-MSI and label free LC–ESI-MS/MS shotgun proteomics to investigate protein induction in a murine fibrosarcoma model following treatment with a vascular disrupting agent.

An Ebook chapter  “Oncology bioanalysis: from biomarkers to drug discovery” was co-written with Prof Malcolm Clench, for a book entitled; Oncological Imaging tools in Mass Spectrometry. The latter providing current opinion and insight in MS as an oncological imaging modality. These outputs have been of great importance to the field of cancer biology, particularly with regards promoting MS analytical techniques in that field.

Describe the most difficult challenge you have encountered in the laboratory and how you overcame it.

The most difficult challenges I have encountered within the bioanalytical laboratory have been the improvisation and changes to my research plan to accommodate the breakdown and repair of the sophisticated instrumentation required for analysis. I have overcome such potential disruption to my research schedules by undertaking alternative experimental validation methods. One such example is spending time optimizing immunohistochemical protocols for the staining of a protein target identified in a recent shotgun proteomics experiment. Responsiveness to change is one of my strengths, an attribute that I regard to be an invaluable asset to a productive research environment.

Where do you see your career in bioanalysis taking you?

I am currently working towards fellowship HE accreditation status within the institution where I currently work. I would therefore like to continue down the career path towards securing my own lectureship post which will enable me to progress to Principle lecturer/Investigator, and eventually supervise my own bioanalytical research team. I have particular expertise in MALDI profiling and imaging and conventional proteomic analysis research encompassing nLC–ESI and LC–MALDI but I am interested in all analytical techniques; particularly using a combination of biochemistry and analytical techniques as discovery tools for proteomic, lipid and metabolite analysis. I am passionate about knowledge transfer and would encourage students. I would aim to achieve a fusion of teaching enhanced by my research interests to contribute to the growing knowledge and research in the field of innovative analytical science.

How do you envisage the field of bioanalysis evolving in the future?

One of my research interests is the use of alternative disease models to assess response to anti-cancer treatment. In acknowledgement of the initiative to reduce, refine and replace the requirement for animal models in research, studying sections of 3D organoid tissue generated from human cell lines with various bioanalytical techniques would allow visualization of a proteomic, lipidomic or metabolomic molecular ‘snapshot’. I believe that using 3D organoid disease models would provide a multitude of possibilities for the study of many diseases employing bioanalytical techniques, in order to mimic in vivo environments. In the future, these models could be representative knockdown 3D organoids, containing multi-populations of cells, with the purpose of mimicking invivo response to treatment. Tissue culture and MS techniques would aim to help define regions of interest containing such populations. Comparative studies using 3D living skin culture systems with monolayer equivalents would also make interesting future publications.

Please list 5 of your recent publications, and select one that best highlights your career to date in the field of bioanalysis.

Cole LM, Bluff JE, Carolan VA,  Paley MN, Tozer GM, Clench MR. MALDI-MSI and Label free LC-ESI-MS/MS Shotgun Proteomics to Investigate Protein Induction in a Murine Fibrosarcoma Model following Treatment with a Vascular Disrupting Agent. Proteomics. DOI: 10.1002/pmic.201300429 (2014) (Epub ahead of print).

Cole LM, Tozer GM, Smith DP, Clench MR. Recombinant “IMS TAG” Proteins – A new method for validating bottom up matrix assisted laser desorption – ion mobility separation – mass spectrometry imaging (MALDI-IMS-MSI). Rapid Communications in Mass Spectrometry. 27(21), 2355–2362 (2013).

Cole LM, Djidja M-C, Bluff J , Claude E, Carolan VA, Paley M , Tozer GM, Clench MR. Investigation of protein induction in tumour vascular targeted strategies by MALDI MSI. Methods. 54, 442–453 (2011).

Mahmoud K, Cole LM, Newton J et al. Detection of EGFR, Epiregulin and Amphiregulin in Formalin Fixed Paraffin Embedded Human Placental Tissue by MALDI-MS Imaging. European Journal of Mass Spectrometry. 19(1), 17–28 (2013)

Trim PJ, Djidja M-C, Muharib T et al. Instrumentation and software for mass spectrometry imaging—Making the most of what you’ve got. Journal of Proteomics. 75(16), 4931–4940 (2012).

First choice: Cole LM, Bluff JE, Carolan VA,  Paley MN, Tozer GM, Clench MR. MALDI-MSI and Label free LC-ESI-MS/MS Shotgun Proteomics to Investigate Protein Induction in a Murine Fibrosarcoma Model following Treatment with a Vascular Disrupting Agent. Proteomics. DOI: 10.1002/pmic.201300429 (2014) (Epub ahead of print).

Reasoning: My research outputs over the last 5 years are publications which involve MS imaging development and a variety of other analytical techniques as biomarker discovery tools (including potential pharmacological targets that could be the focus of future drug design). The rationale for my selection of the above publication is that this work to date is a collaboration of key complementary bioanalytical techniques, each with the aim of providing cross validation of proteomic drug treatment responses.