Albert J.R. Heck (born 25 November 1964) is a Dutch scientist and professor at Utrecht University, the Netherlands in the field of mass spectrometry and proteomics. He is known for his work on technologies to study proteins in their natural environment, with the aim to understand their biological function. Albert Heck was awarded the Spinoza Prize in 2017, the highest scientific award in the Netherlands.
In 1998 he accepted a chair at Utrecht University as head of the Biomolecular Mass Spectrometry and Proteomics Group.[1] His group is part of the Departments of Chemistry and Pharmaceutical Sciences of the Faculty of Science.[2] From 2006 until 2012 Heck was scientific director of the Bijvoet Centre for Biomolecular Research, and from 2015 to 2018 scientific director of the Utrecht Institute for Pharmaceutical Science at Utrecht University. In 2017 he received a Distinguished Faculty professorship of Utrecht University.[3]
Research
The research of Albert Heck is focused on the development and use of mass spectrometry to study all cellular proteins. Within his research group, there are three main lines of research, improvement of instrumentation and analytical methods, proteomics and mass spectrometry based structural biology, including native protein mass spectrometry and cross-linking mass spectrometry.
Albert Heck is regarded as one of the pioneers of native mass spectrometry.[4][5][6] Among the complexes that he studied using native mass spectrometry are intact viruses of up to 18 megadalton,[7][8]ribosomes,[9]antibodies in complex with their antigens[10] or proteins of the complement system.[11][12] He has developed, in collaboration with Alexander Makarov mass spectrometers with extended mass ranges, specifically suited for the analyses of very large protein complexes, which were later commercialized by the company ThermoFisher Scientific as the Orbitrap EMR and UHMR.
In proteomics, Heck is most renowned for his work on quantitative proteomics,[13][14] interactomics,[15] and the analysis of post-translational modification of proteins using mass spectrometry, with a focus on protein phosphorylation[16] and protein glycosylation.[17] This started with the introduction of the material TiO2 as a method for the targeted analysis of phosphopeptides in 2004.[18] The methods developed by Heck have been adopted by many scientists in other fields, to study how protein expression and phosphorylation are regulated in human cells and tissues by different biological processes and disease states.[19][20]
Additionally, he advocated the use of complementary proteases in shot-gun proteomics[21][22] and he introduced and developed novel peptide fragmentation strategies to elucidate site specific post-translational modifications.[23] The latter improves determination of peptide and protein sequence information, which is particular helpful for the analysis of glycopeptides[24] and HLA antigens.[25][26] Heck also contributed to the field of cross-linking mass spectrometry, through proteome wide cross-linking experiments,[27] and the development of novel fragmentation methods and the software suite XlinkX.[28]
Albert Heck is closely involved in coordinating access to proteomics infrastructures in the Netherlands and in Europe. Since 2003 Heck is scientific director of the Netherlands Proteomics Centre.[29] From 2011 to 2015 he was coordinator of PRIME-XS,[30] and since 2019 he coordinates EPIC-XS,[31] both collaborative projects funded by the European Union to enable access to proteomics technology for researchers throughout Europe.
Honours and awards
Heck received numerous awards and prizes for his scientific contributions. He received The KNCV golden medal in 2001,[32] the Descartes-Huygens Prize from the Académie de Sciences in 2006,[33] the Life Science Award of the German Mass Spectrometry Society in 2010, the Discovery Award in Proteomic Sciences from the Human Proteome Organization in 2013[34] and the UePA Pioneer Proteomics Award in 2014.
In 2017, he was awarded the Spinoza Prize, the highest scientific distinction in the Netherlands for his "major contribution to the worldwide breakthrough of systematically mapping all proteins in human cells and their biological functions by means of mass spectrometry".[39]
^Krijgsveld, Jeroen; Ketting, René F.; Mahmoudi, Tokameh; Johansen, Janik; Artal-Sanz, Marta; Verrijzer, C. Peter; Plasterk, Ronald H. A.; Heck, Albert J. R. (2003). "Metabolic labeling of C. Elegans and D. Melanogaster for quantitative proteomics". Nature Biotechnology. 21 (8): 927–931. doi:10.1038/nbt848. PMID12858183. S2CID2641430.
^Boersema, Paul J.; Raijmakers, Reinout; Lemeer, Simone; Mohammed, Shabaz; Heck, Albert J. R. (2009). "Multiplex peptide stable isotope dimethyl labeling for quantitative proteomics". Nature Protocols. 4 (4): 484–494. doi:10.1038/nprot.2009.21. PMID19300442. S2CID5498505.
^"Moeilijk te vangen fosforgroepen" (in Dutch). Chemisch2Weekblad (C2W) Life Sciences. 23 June 2012.
^Yang, Yang; Franc, Vojtech; Heck, Albert J.R. (2017). "Glycoproteomics: A Balance between High-Throughput and In-Depth Analysis". Trends in Biotechnology. 35 (7): 598–609. doi:10.1016/j.tibtech.2017.04.010. hdl:1874/351003. PMID28527536.
^Pinkse, Martijn W. H.; Uitto, Pauliina M.; Hilhorst, Martijn J.; Ooms, Bert; Heck, Albert J. R. (2004). "Selective Isolation at the Femtomole Level of Phosphopeptides from Proteolytic Digests Using 2D-NanoLC-ESI-MS/MS and Titanium Oxide Precolumns". Analytical Chemistry. 76 (14): 3935–3943. doi:10.1021/ac0498617. PMID15253627.
^Giansanti, Piero; Tsiatsiani, Liana; Low, Teck Yew; Heck, Albert J. R. (2016). "Six alternative proteases for mass spectrometry–based proteomics beyond trypsin". Nature Protocols. 11 (5): 993–1006. doi:10.1038/nprot.2016.057. hdl:1874/333986. PMID27123950. S2CID2597839.
^Frese, Christian K.; Altelaar, A. F. Maarten; Van Den Toorn, Henk; Nolting, Dirk; Griep-Raming, Jens; Heck, Albert J. R.; Mohammed, Shabaz (2012). "Toward Full Peptide Sequence Coverage by Dual Fragmentation Combining Electron-Transfer and Higher-Energy Collision Dissociation Tandem Mass Spectrometry". Analytical Chemistry. 84 (22): 9668–9673. doi:10.1021/ac3025366. PMID23106539.
^Reiding, Karli R.; Bondt, Albert; Franc, Vojtech; Heck, Albert J.R. (2018). "The benefits of hybrid fragmentation methods for glycoproteomics". Trends in Analytical Chemistry. 108: 260–268. doi:10.1016/j.trac.2018.09.007. hdl:1874/373361. S2CID105377340.
^Liepe, Juliane; Marino, Fabio; Sidney, John; Jeko, Anita; Bunting, Daniel E.; Sette, Alessandro; Kloetzel, Peter M.; Stumpf, Michael P. H.; Heck, Albert J. R.; Mishto, Michele (2016). "A large fraction of HLA class I ligands are proteasome-generated spliced peptides". Science. 354 (6310): 354–358. Bibcode:2016Sci...354..354L. doi:10.1126/science.aaf4384. hdl:10044/1/42330. PMID27846572. S2CID41095551.
^Liu, Fan; Rijkers, Dirk T. S.; Post, Harm; Heck, Albert J. R. (2015). "Proteome-wide profiling of protein assemblies by cross-linking mass spectrometry". Nature Methods. 12 (12): 1179–1184. doi:10.1038/nmeth.3603. hdl:1874/329447. PMID26414014. S2CID6786537.