It is with heavy hearts that we write to inform you that our dear colleague Toby (Torbjorn) Jarbe passed away on Wednesday November 16th, 2016. We will keep him in our hearts and he will always be remembered for the joyful, sarcastic, and inspiring scientist that he was known to be. It is without saying that he made his mark within the Center for Drug Discovery, as well as on our hearts. He will be missed and forever remembered.
Please join the CDD in celebrating Toby Jarbe’s life and accomplishments on Monday December 19th, 2016 from 4:00 pm -5:00 pm at The Fenway Center @ Northeastern – 77 St. Stephen Street, Boston, MA, 02115
Questions: Please contact Amanda DiCristoforo 617-373-7866 / email@example.com
Major Research Areas
The Endocannabinoid Biochemical System in Drug Discovery: Cannabinergic drugs modulate the central nervous and immune systems by acting through two receptors (CB1; CB2) and two classes of endogenous ligands represented by anandamide and 2-arachidonyl glycerol (endocannabinoids). The endocannabinoid system is further regulated by the inactivating enzyme, fatty acid amide hydrolase (FAAH), and a newly discovered transport system. We are studying the interactions of cannabinergic ligands with the above receptors, enzymes and transporters using a combination of chemical, biochemical, biophysical and computational methods. Our results are further used to design and synthesize novel therapeutically useful drugs for pain, appetite and central nervous system diseases.
Ligand Assisted Protein Structure (LAPS): This novel approach for studying the structural features involved in the interaction of a ligand (drug) with its target protein was developed within the CDD. It involves the design and development of highly selective ligands capable of interacting covalently with a functional protein (GPCR, enzyme, transporter). The ligand-protein binding motif is obtained through the combined use of protein mutants in combination with proteomic methods for characterizing the amino acid residues involved in ligand attachment at the protein binding site. The information offered is used to model the drug-protein complex by computer modeling. The results are used as a basis for the design and development of new medications.
Our research is well supported by NIH grants and offers opportunities for training in model medicinal chemistry.
Choices of projects within the Center for Drug Discovery include:
- Drug design and synthesis
- Chemical/biochemical approaches including LC/MS for studying drug:receptor interactions
- NMR and other biophysical methods for drug design and discovery
Mass Spectrometry at the CDD
The Center for Drug Discovery offers access to a nano-LC- 4000 QTrap (Applied Biosystems) with an ESI source and a TSQ Quantum Ultra Triple Quadrupole (Thermo Scientific) mass spectrometer with both ESI and APCI ion sources and an Agilent 1100 LC frontend.
The Center for Drug Discovery Mass Spectrometry laboratory has an ABI QTRAP 4000 mass spectrometer with a nano-LC-MS system on the front end. This state-of-the-art instrument is the only hybrid quadrupole linear ion trap available on the market and it is extremely sensitive for both protein identification and characterization and small molecule quanitification. The split-less nano-LC has an exceptionally stable flow rate for reproducible gradients. This nano-LC system allows us to do multi-dimensional chromatography where ion exchange chromatography or on-line sample clean-up can be performed prior to reverse phase chromatography.
The Center for Drug Discovery Mass Spectrometry laboratory has a Thermo-Finnigan TSQ Quantum Ultra triple quad mass spectrometer, complete with an Agilent 1100 front end. This instrument has the widest linear dynamic range and highest sensitivity of any triple quad currently on the market, demonstrating detection of our compounds down to the femtogram level. This instrument is equipped with both an ESI and APCI source and includes metabolite ID software to enhance our pharmacokinetic capabilities.
Please contact Amanda DiCristoforo for rates and availability.