Sunday, April 23rd, 2017

Meetings

April 2017 Meeting

Speaker: Lisa Jones, University of Maryland School of Pharmacy

Topic: Extension of Hydroxyl Radical-Based Footprinting Coupled with Mass Spectrometry for In Cell and In Vivo Protein Analysis

Date: Monday, April 17, 2017

Time: 6:15 pm Dinner, 7:15 pm: Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Katherine Fiedler (Katherine.L.Fiedler@fda.hhs.gov) before April 17 if you will be attending the dinner or are a presenting as a vendor.

Abstract: In recent years, protein footprinting coupled with mass spectrometry has been used to identify protein-protein interaction sites and regions of conformational change through modification of solvent accessible sites in proteins. Hydroxyl radical-based footprinting (HRBF) approaches utilize hydroxyl radicals to oxidatively modify the side chains of solvent accessible amino acids. There are several approaches to generate radicals for oxidation including synchrotron radiation and electrochemistry. One HRBF method, fast photochemical oxidation of proteins (FPOP), utilizes an excimer laser for photolysis of hydrogen peroxide to generate hydroxyl radicals. To date, HRBF methods have been used in vitro on relatively pure protein systems. We have further extended the FPOP method for in cell analysis of proteins. This will allow for study of proteins in their native cellular environment and be especially useful for the study of membrane proteins which can be difficult to purify for in vitro studies. We have designed and built a single cell flow system to enable uniform access of cells to the laser. Results demonstrate that in cell FPOP (IC-FPOP) can oxidatively modify over 1300 proteins in various cellular compartments. Further, the method successfully probes solvent accessibility similarly to in vitro FPOP. We have further extended the method for in vivo analysis using C. elegans, members of the nematode family. C. elegans are widely used as model systems for human diseases including cancer, Parkinson’s disease, and diabetes. Preliminary results indicate a number of proteins can be oxidatively modified in C. elegans by in vivo FPOP (IV-FPOP) leading to the possibility of studying protein structure in human diseases directly in animal model systems. However, further optimization of the method is required to increase the number of oxidatively modified proteins.

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The 11th Summer School for “Mass Spectrometry in Biotechnology and Medicine” (MSBM)

Date: July 2-8, 2017

The 11th Edition of the Summer School for “Mass Spectrometry in Biotechnology and Medicine” (MSBM), will be held at the Centre for Advanced Academic Studies (CAAS), Dubrovnik, Croatia, 2-8 July 2017. Once again MSBM features instruction by the leading international scientists in mass spectrometry. However, this year MSBM is working together with the Nederlandse Vereniging voor Massaspectrometrie (NVMS) to host the third International Mass Spectrometry School (IMSS-2017) on behalf of the International Mass Spectrometry Foundation (IMSF).

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March 2017 Meeting

Speaker: Robert N. Cole, Johns Hopkins School of Medicine

Topic: Adventures of Capillary Electrophoresis in Proteomics, from Top-down to Bottom-up

Date: Monday, March 27, 2017

Time: 6:15 pm Dinner, 7:15 pm: Presentation

Location: Shimadzu Scientific Instrument, Inc. Training Center 7100 Riverwood Drive, Columbia, MD 21046 (Directions)

Dinner: Please RSVP to Katherine Fiedler (Katherine.L.Fiedler@fda.hhs.gov) before February 27 if you will be attending the dinner or are a presenting as a vendor.

Abstract: Capillary zone electrophoresis (CE)-MS has become more accessible with robust electrospray interfaces, presenting a potential alternative to LC-MS. CE achieves rapid and high resolution analyte separation based on net charge and hydrodynamic volume. CE is orthogonal to reversed phase LC with additional benefits of low carryover, low (nanogram) sample injection, and rapid sample loading. CE-MS analysis of complex peptide mixtures is challenging due to the seconds-wide elution peaks produced during the rapid separations. However, increases in MS data acquisition speeds warrant re-examination of the role of CE in proteomics. We are evaluating a microfluidic chip-based CE interface (ZipChip, 908 Devices Inc) for top-down analysis of intact proteins, analysis of high charge/high pI peptides, and bottom-up quantification of proteins. Even with major challenges of sample concentration, protein complexity and automation, CEMS has a bright future in protein analysis.

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