Adrian Whitty

Whitty, Adrian

Professor Adrian Whitty

Prior to joining the Boston University faculty in 2008, Adrian Whitty worked for 14 years at Biogen Idec (then Biogen Inc.).  He rose from staff Scientist to the position of Director in the Drug Discovery Department and Head of Physical Biochemistry, leading a department that encompassed Quantitative Biochemistry, Assay Development and Compound Profiling, Structural Biology, and Molecular Modeling. During his time at Biogen Idec Prof. Whitty participated in or led multiple drug discovery project teams. He also maintained an active research program in the areas of receptor signaling and protein-ligand binding. He additionally directed the Biogen Idec Postdoctoral Program, developing a sterling reputation as a post-doctoral mentor.

Degrees and Positions

  • B.Sc. (Hon) in Chemistry, King’s College, University of London, 1985
  • Ph.D. in Organic Chemistry, University of Illinois at Chicago, 1991
  • Postdoctoral Research Fellow, Brandeis University, Graduate Department of Biochemistry, 1990-93
  • Membership Committee, The Protein Society, 2008-present
  • Member, Governing Council, American Society of Biochemistry and Molecular Biology (ASBMB), 2007-present
  • Founding Member, Council for Systems Biology in Boston (CSB2), 2007-present

  • Advisory Board Member, Institute for Chemical Biology and Drug Discovery, SUNY Stony Brook (2004-present)
  • Co-Chair, 2002 Gordon Research Conference on Bioorganic Chemistry


  • Director, Physical Biochemistry (2/07-4/08), Associate Director & Head, Physical Biochemistry (1/03-1/07), Biogen Idec Inc., Cambridge, MA
  • Senior Scientist (1999-2002), Drug Discovery Department, Biogen Inc. Cambridge, MA
  • Director, Biogen Idec Postdoctoral Program, 2005-4/08
  • Cited in Science as a top postdoc mentor (“Success Factors for Postdocs”, Sept 17, 2004)


Science cited Prof. Whitty as one of the top post-doctoral mentors in the country.

The Whitty Group studies protein-protein and protein-ligand recognition, with an emphasis on how binding energy from these intermolecular interactions can be utilized to achieve biological function or inhibition.  We apply this research in two distinct areas: (i) developing a quantitative, mechanistic understanding of the activation and signaling of growth factor receptors, and (ii) advancing our ability to discover drugs that inhibit protein-protein interactions.

  • Activation and signaling mechanisms in growth factor receptor systems. This work aims to address longstanding mechanistic questions concerning exactly how the binding of a cytokine or growth factor brings about an activated state of its receptor, and how the assembly of the activated receptor complex is quantitatively coupled to proximal and distal signaling events and to the ultimate cellular response (See Schlee et al., Nature Chemical Biology, 2006).
  • Research image

    The protein-protein interaction between NEMO and IKK, with the target site for inhibition highlighted by modeled fragment clusters (cyan and magenta stick representations)

    Discovery and characterization of small molecule (i.e. synthetic organic) inhibitors of protein-protein interactions. We aim to develop new approaches to this difficult problem, based on achieving a better understanding of what structural and physicochemical properties at protein-protein interfaces are important for inhibitor binding, and what kinds of novel chemical structures are best suited to exploit these features. Projects in this area are carried out in collaboration multiple other groups encompassing computational chemistry (Prof. Vajda), organic synthesis (Profs. Porco, Beeler, CMLD-BU; Prof. Pollastri, Northeastern U.), X-ray crystallography (Prof. Allen) and Biology (Prof. Gilmore, BU Department of Biology).

Techniques & Resources

  • Development and implementation of biochemical and cell-based assays using state-of-the art technologies such as FRET, Time-Resolved Fluorescence, and Fluorescence Polarization.
  • Biophysical methods – the lab is equipped with a Biacore 3000 surface plasmon resonance (SPR) instrument for measuring protein-ligand binding in real time. Other biophysical methods used include fluorescence, analytical ultracentrifugation (AUC), dynamic lightscattering (DLS) and isothermal titration calorimetry (ITC).
  • Mammalian Cell Culture – the lab has a dedicated Tissue Culture facility equipped with laminar flow biosafety cabinet, cell incubators, centrifuge, Nikon inverted microscope, and liquid nitrogen cell storage system.
  • Specialized techniques for cell analysis (e.g. flow cytometry using a Becton-Dickinson FACSCaliburTM)
  • Quantitative data analysis, curve fitting and reaction pathway modeling using a variety of software packages including site licenses to MathematicaTM and MatLab®.


Projects in the Whitty lab often involve collaboration with scientists from different backgrounds and disciplines. For example, our work aimed at identifying macrocyclic inhibitors of NEMO provides opportunities to participate in a multidisciplinary team involving computational chemists, synthetic organic chemists, X-ray crystallographers and biologists, providing broad exposure to how these different disciplines contribute to drug discovery.

Several projects in the Whitty lab provide the opportunity to interact or even collaborate with scientists from various pharmaceutical companies.

What’s Next for Graduates of the Whitty Group?

The Whitty Group’s training in rigorous, hypothesis-driven experimental design and interpretation prepares students for future careers in either academia or industry.  The group is quite new, and so no students have yet graduated. However, a postdoctoral research fellow, Dr. Tom Riera, recently left the group to take a position as Senior Scientist at Sirtris Pharmaceuticals.

Associate Professor
SCI 359
Fax: 617.353.6466
Google Scholar Page
Office Hours: by Appointment
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