My Work - Scientific Research Papers
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Below is a list of my scientific publications. You can access links to the articles from my Google Scholar profile.
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RESEARCH OVERVIEW
I have spent the past eight years of my career in the fields of biocatalysis and synthetic biology, working both in industry and academia. My work has focused on engineering various enzymes (carboxylic acid reductases, alcohol dehydrogenases, ene-reductases and lipases) to be used as biocatalysts in the pharmaceutical, flavors, fragrances and food industries. The methodologies I have used and helped to develop, range from the creation of smart libraries of mutants to the development of high-throughput screenings to select for the improved mutants. My projects have always been co-funded by industry (GSK and DSM), a testimony to their applied interest.
Having worked in the first start-up company in the UK dedicated to synthetic biology (Synthace) has helped me to better understand the challenges we still need to overcome to transform biology into the engineering discipline of the future – in particular, issues of data reproducibility and big data management. |
LIST OF PUBLICATIONS
Quaglia, D., Alejaldre, L., Ouadhi, S., Rousseau, O. & Pelletier, J. N. (2019) Holistic engineering of Cal-A lipase chain-length selectivity identifies triglyceride binding hot-spot. PLoS ONE 14, e0210100–17 L. T. Chisty, D. Quaglia, M. R. Webb (2018) - Fluorescent single-stranded DNA-binding protein from Plasmodium Falciparum as a biosensor for single-stranded DNA - PLoS ONE 13(2): e0193272. A. J. L. Wood, N. J. Weise, J. D. Frampton, M. S. Dunstan, M. A. Hollas, S. R. Derrington, R. C. Lloyd, D. Quaglia, F. Parmeggiani, D. Leys, N. J. Turner, S. L. Flitsch (2017) – Adenylation activity of carboxylic acid reductases enables the synthesis of amides - Angew. Chem. 129 (46): 14690-14693. d.o.i: 10.1002/ange.201707918 D. Galoth, M. S. Dunstan, D. Quaglia, E. Klumbys, M. P. Lockhart-Cairns, A. M. Hill, S. R. Derrington, N. S. Scrutton, N. J. Turner, D. Leys (2017) - Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis – Nature Chemical Biology 13, 975–981 doi:10.1038/nchembio.2434 N. M. Rachel, D. Quaglia, E. Lévesque, A. B. Charette, J. N. Pelletier (2017) - Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements. Protein Science, 26: 2268–2279. doi:10.1002/pro.3286 D. Quaglia, M. Ebert, P. F. Mugford, J. N. Pelletier (2017) – Enzyme engineering: a synthetic biology approach for more effective library generation and automated high-throughput screening – PLoS ONE 12, e0171741 D. Quaglia, M. Pori, P. Galletti, E. Emer, F. Paradisi, D. Giacomini (2013) - His-Tagged Horse Liver Alcohol Dehydrogenase: Immobilization and application in the bio-based enantioselective synthesis of (S)-arylpropanols – Process. Biochem., 48:818-818, D.O.I. 10.1016/j.procbio.2013.03.016 F. Hackenberg, G. Lally, H. Müller-Bunz; F. Paradisi, D. Quaglia, W. Streciwilk, M. Tacke (2013) - Synthesis and biological evaluation of N-heterocyclic carbene-silver(I) acetate complexes derived from 4,5-ditolyl-imidazole, Inorg. Chim. Acta, 395:135-144, D.O.I. 10.1016/j.ica.2012.10.029 D. Quaglia, J. A. Irwin, F. Paradisi (2012) - Horse Liver Alcohol Dehydrogenase: new perspectives for an old enzyme - Mol. Biotechnol., 52:244-250, D.O.I. 10.1007/s12033-012-9542-7 F. Hackenberg, G. Lally, H. Müller-Bunz, F. Paradisi, D. Quaglia, W. Streciwilk, M. Tacke (2012) - Novel symmetrically p-benzyl-substituted 4,5-diaryl-imidazole N-heterocyclic carbene-silver(I) acetate complexes: synthesis and biological evaluation - J. Organomet. Chem., pp 123-134, D.O.I. 10.1016/j.jorganchem.2012.07.006 F. Hackenberg, A. Deally, G. Lally, S. Malenke, H. Müller-Bunz, F. Paradisi, S. Patil, D. Quaglia and M. Tacke (2012) - Novel non-symmetrically p-benzyl-substituted (benz)imidazole N-heterocyclic carbene-silver(I) acetate complexes: synthesis and biological evaluation - Int. J. Inorg. Chem, volume 2012, 13 pages, Article ID 12154, D.O.I. 10.1155/2012/121540 |