David Goodlett
Professor, Biochemistry & Microbiology, University of Victoria
phone: 250.721.7242
email: goodlett@uvic.ca
About David Goodlett
Dave is currently Professor of Biochemistry and Microbiology at the University of Victoria where he is also Director of the Genome BC Proteome Centre (https://www.proteincentre.com/). He is also a Mentor for the Chemical Biology group at the University of Gdansk’s International Centre for Cancer Vaccine Science (https://iccvs.ug.edu.pl/). Previously he was a Professor at the University of Maryland in Baltimore, MD (2013-2020). From 2012-2016 he was a Finland Distinguished Professor (FiDiPro) at the University of Turku in Turku, Finland. The research at the University of Turku was focused on discovery of serum protein markers that predict children who will develop type-1 diabetes prior to appearance of autoantibodies as well as cardiovascular disease in young Finns. More details of the FiDiPro projects are available here. From 2013 to 2016 Dave was the Isaac E. Emerson Professor of Pharmaceutical Sciences at the University of Maryland School of Pharmacy and from 2013-2015 he was Director of the UMB School of Pharmacy MS Center. From 2004-2012 he was Professor of Medicinal Chemistry at the University of Washington in Seattle, WA where he was also Director of the School of Pharmacy mass spectrometry facility.
His research includes hypothesis generating, discovery based efforts in protein and lipid A structure-function relationships in infectious organisms, proteomics technology development and informatics. Prior to his nine-year term at the University of Washington, he was Director of the Institute for Systems Biologyâ„¢ Proteomics laboratory (2000-2003). After postdoctoral work with Richard D. Smith at Pacific Northwest National Laboratory (1991-1993), he spent five years in the pharmaceutical industry and prior to that received his Ph.D. in 1991 with Richard B. van Breemen and Frank B. Armstrong (deceased) at North Carolina State University.
Originally, he was trained as a protein chemist at Auburn University with John Aull, Harlow Daron (deceased) and Frank Bartol. This training in structure-function relationships led to an eventual interest in the same concept for lipid A as it pertains to human health that he has investigated using mass spectrometry. His current efforts are supported by several burgeoning technology projects in mass spectrometry and microfluidics, as well as software development to support structure analysis and –omic pipelines. The discovery based science projects within the laboratory are used to generate hypotheses complementary to those generated by literature review in support of our medical and biological collaborators. In general, we take an indolent driven approach to experimentation that seeks parsimony in data acquisition and interpretation.Additionally, the structure-function relationships of lipid A as it pertains to human health have been investigated by my laboratory using mass spectrometry. All of these efforts are supported by several burgeoning technology projects in mass spectrometry and microfluidics, as well as software development to support structure analysis and –omic pipelines. The discovery based science projects within the laboratory are used to generate hypotheses complementary to those generated by literature review in support of our medical and biological collaborators. In general, we take an indolent driven approach to experimentation that seeks parsimony in data acquisition and interpretation.
His research includes hypothesis generating, discovery based efforts in protein and lipid A structure-function relationships in infectious organisms, proteomics technology development and informatics. Prior to his nine-year term at the University of Washington, he was Director of the Institute for Systems Biologyâ„¢ Proteomics laboratory (2000-2003). After postdoctoral work with Richard D. Smith at Pacific Northwest National Laboratory (1991-1993), he spent five years in the pharmaceutical industry and prior to that received his Ph.D. in 1991 with Richard B. van Breemen and Frank B. Armstrong (deceased) at North Carolina State University.
Originally, he was trained as a protein chemist at Auburn University with John Aull, Harlow Daron (deceased) and Frank Bartol. This training in structure-function relationships led to an eventual interest in the same concept for lipid A as it pertains to human health that he has investigated using mass spectrometry. His current efforts are supported by several burgeoning technology projects in mass spectrometry and microfluidics, as well as software development to support structure analysis and –omic pipelines. The discovery based science projects within the laboratory are used to generate hypotheses complementary to those generated by literature review in support of our medical and biological collaborators. In general, we take an indolent driven approach to experimentation that seeks parsimony in data acquisition and interpretation.Additionally, the structure-function relationships of lipid A as it pertains to human health have been investigated by my laboratory using mass spectrometry. All of these efforts are supported by several burgeoning technology projects in mass spectrometry and microfluidics, as well as software development to support structure analysis and –omic pipelines. The discovery based science projects within the laboratory are used to generate hypotheses complementary to those generated by literature review in support of our medical and biological collaborators. In general, we take an indolent driven approach to experimentation that seeks parsimony in data acquisition and interpretation.
Research Interests
Fundamentally Dave’s interest in science revolves around the conundrum of structure-function relationships. Historically, he has used mass spectrometry to pursue this interest and recently, which led to involvement in the investigation of early protein markers of lung diseases and leukemia classification as well as use of chemical cross-linking to ascertain juxtaposed faces of interacting proteins. Additionally, the structure-function relationship of immunologically active lipids pertinent to human health and disease are being investigated using mass spectrometry. All of these efforts are supported by several burgeoning technology projects in mass spectrometry and microfluidics, as well as software development to support structure analysis and –omic pipelines. The discovery based science projects within the laboratory are used to generate hypotheses complementary to those generated by literature review in support of our medical and biological collaborators. In general we take an indolent driven approach to experimentation that seeks parsimony in data acquisition and interpretation. All of my graduate students have a co-mentor whose biomedical problem we develop novel methods to solve.
Most of Dave’s career has been spent working on team-based, collaborative science projects where his laboratory’s role was to provide analytical solutions to solve biomedical problems. Specifically, his laboratory conducts bioanalytical research using methods tailored to solve biologic and medical problems using mass spectrometry, particularly related to protein and lipid function. This focus is reflected in many of the lab’s most recent publications on proteome characterization that focus on the data-independent precursor acquisition independent from ion count (PAcIFIC) method that systematically profiles all mass/charge (m/z) channels. The PAcIFIC method extends detectable dynamic range by systematically profiling ever m/z channel in a data independent manner without regard to detection of precursor ions. To further extend detectable dynamic range we have worked with Spectroglyph (Kennewick, WA) to assemble a bespoke ion mobility quadrupole Exactive Oribtrap (unpublished data).
In support of our efforts to analyze proteins, proteomes and glycolipids, the lab has published a number of novel software solutions and where possible have used in silico modeling to confirm/refute experimental hypotheses. Specifically, software solutions include three unique methods for assignment of chemical cross-links in individual proteins and/or multi-protein complexes each of which may also be used to detect and map post-translationally modified sites on proteins. Most recently the lab has used these methods to study mono- and poly-ADP-ribosylation. Dave’s lab has also developed software and mass spectrometry methods for determination of bacterial gylcolipid structures.
With regard to translation of our ideas Dave has been involved in the creation of two companies. Deurion LLC of Seattle, WA spun out in 2011 from the University of Washington to develop surface acoustic wave nebulization (SAWN) as an ion source for mass spectrometry and 2) Pataigin LLC of Baltimore, MD spun out in 2016 from the University of Maryland to develop novel methods for bacterial identification and therapeutics based around the activity of the Gram-negative membrane glycolipid known as lipid A. Deurion has raised approximately one million in SBIR funding to develop SAWN and has recently begun to market a product for use with select mass spectrometers. Pataigin is in the early stages of licensing intellectual property and forming alliances with larger companies who are interested in the Pataigin’s direct from sample bacterial identification process.
To conclude, one of the central foci of the lab has been inflammation in chronic human diseases and microbial pathogenesis. The latter research focus is built around development of a structure activity relationship (SAR) library for lipid A with the goal of developing better vaccine adjuvants and anti-sepsis molecules. Specifically, this work involves discovery of novel glycolipids and their structures from marine sponges and extremophiles as well as mapping the downstream proteomic changes in macrophages as a result of select lipid A molecules binding to the MD2/TLR4 complex. The work in chronic human diseases has most recently involved clinical proteomic analysis of longitudinal samples from Finnish biobanks in pediatric type-1 diabetes and cardiovascular disease. Moving forward the key technologies being used for success in the laboratory are top-down proteomics and mass spectrometry imaging.
Fundamentally Dave’s interest in science revolves around the conundrum of structure-function relationships. Historically, he has used mass spectrometry to pursue this interest and recently, which led to involvement in the investigation of early protein markers of lung diseases and leukemia classification as well as use of chemical cross-linking to ascertain juxtaposed faces of interacting proteins. Additionally, the structure-function relationship of immunologically active lipids pertinent to human health and disease are being investigated using mass spectrometry. All of these efforts are supported by several burgeoning technology projects in mass spectrometry and microfluidics, as well as software development to support structure analysis and –omic pipelines. The discovery based science projects within the laboratory are used to generate hypotheses complementary to those generated by literature review in support of our medical and biological collaborators. In general we take an indolent driven approach to experimentation that seeks parsimony in data acquisition and interpretation. All of my graduate students have a co-mentor whose biomedical problem we develop novel methods to solve.
Most of Dave’s career has been spent working on team-based, collaborative science projects where his laboratory’s role was to provide analytical solutions to solve biomedical problems. Specifically, his laboratory conducts bioanalytical research using methods tailored to solve biologic and medical problems using mass spectrometry, particularly related to protein and lipid function. This focus is reflected in many of the lab’s most recent publications on proteome characterization that focus on the data-independent precursor acquisition independent from ion count (PAcIFIC) method that systematically profiles all mass/charge (m/z) channels. The PAcIFIC method extends detectable dynamic range by systematically profiling ever m/z channel in a data independent manner without regard to detection of precursor ions. To further extend detectable dynamic range we have worked with Spectroglyph (Kennewick, WA) to assemble a bespoke ion mobility quadrupole Exactive Oribtrap (unpublished data).
In support of our efforts to analyze proteins, proteomes and glycolipids, the lab has published a number of novel software solutions and where possible have used in silico modeling to confirm/refute experimental hypotheses. Specifically, software solutions include three unique methods for assignment of chemical cross-links in individual proteins and/or multi-protein complexes each of which may also be used to detect and map post-translationally modified sites on proteins. Most recently the lab has used these methods to study mono- and poly-ADP-ribosylation. Dave’s lab has also developed software and mass spectrometry methods for determination of bacterial gylcolipid structures.
With regard to translation of our ideas Dave has been involved in the creation of two companies. Deurion LLC of Seattle, WA spun out in 2011 from the University of Washington to develop surface acoustic wave nebulization (SAWN) as an ion source for mass spectrometry and 2) Pataigin LLC of Baltimore, MD spun out in 2016 from the University of Maryland to develop novel methods for bacterial identification and therapeutics based around the activity of the Gram-negative membrane glycolipid known as lipid A. Deurion has raised approximately one million in SBIR funding to develop SAWN and has recently begun to market a product for use with select mass spectrometers. Pataigin is in the early stages of licensing intellectual property and forming alliances with larger companies who are interested in the Pataigin’s direct from sample bacterial identification process.
To conclude, one of the central foci of the lab has been inflammation in chronic human diseases and microbial pathogenesis. The latter research focus is built around development of a structure activity relationship (SAR) library for lipid A with the goal of developing better vaccine adjuvants and anti-sepsis molecules. Specifically, this work involves discovery of novel glycolipids and their structures from marine sponges and extremophiles as well as mapping the downstream proteomic changes in macrophages as a result of select lipid A molecules binding to the MD2/TLR4 complex. The work in chronic human diseases has most recently involved clinical proteomic analysis of longitudinal samples from Finnish biobanks in pediatric type-1 diabetes and cardiovascular disease. Moving forward the key technologies being used for success in the laboratory are top-down proteomics and mass spectrometry imaging.
Positions
- 2020-present: Professor of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada
- 2020-present: Director of University of Victoria Genome BC Proteome Centre
- 2019-2020: Professor on sabbatical in UMB’s Dental School, Baltimore, MD
- 2018-present: Visiting Professor & Mentor, University of Gdansk’s ICCVS, Gdansk, Poland
- 2013-2019: Professor of Pharmaceutical Sciences, UMB, Baltimore, MD
- 2013-2016: Isaac E Emerson Professor of Pharmaceutical Sciences, UMB, Baltimore, MD
- 2013-2016: Finland Distinguished Professor, University of Turku, Turku, Finland
- 2013-2015: Director UMB SOP MS Center, Baltimore, MD
- 2008-2013: Professor, Medicinal Chemistry, UW, Seattle, WA
- 2005-2012: Visiting Professor, University of Edinburgh, Edinburgh, UK
- 2007-2012: Director UW SOP MS Center, Seattle, WA
- 2004-2007: Associate Professor, Medicinal Chemistry, UW
- 2000-2003: Director, Proteomics Laboratory, Institute for Systems Biology
- 1997-2000: Visiting Research Scientist, Molecular Biotechnology, UW
- 1995-1997: Res Investigator II, Immunological Diseases, Bristol Myers Squibb, Seattle, WA
- 1993-1994, Res Scientist, Immunobiology Research Institute, J&J, Annandale, NJ
- 1991-1993, NORCUS Fellow, Battelle, Pacific Northwest National Laboratory, Richland, WA
- 1987-1990, Teaching Assistant, Biochemistry, North Carolina State University, Raleigh, NC
- 1984-1986, Technician, Animal Science, Auburn University, Auburn, AL
- 1982-1984, Teaching Assistant, Chemistry, Auburn University
Education
- 1985-1991: Ph.D. in Biochemistry, North Carolina State University, NC.
- 1982-1988: M.S. in Chemistry, Auburn University, Auburn, AL
- 1978-1982: B.S. in Chemistry, Auburn University
- 1975-1978: Robert E. Lee High School, Montgomery, AL
- 1972-1975: Goodwyn Junior High School, Montgomery, AL
- 1966-1972: Dalraida Elementary School, Montgomery, AL