Synthesis on Scale Symposium: Process Chemistry in the Pharmaceutical Industry

Rutgers University Department of Chemistry & Chemical Biology, 123 Bevier Road, Piscataway, NJ, 08854 123 Bevier Road, Piscataway, United States

Presented by the Princeton ACS and Rutgers University. A series of talks will be given on January 12, 2024 from 9:30 to 3:45 pm. Speakers include Harshkumar Patel from Bristol-Myers Squibb, Kevin Campos from Merck, Chris Senanayake from TCG GreenChem, and Prof. Kendall Houk from UCLA. They will cover a range of topics from innovations in synthetic chemistry to computational elucidation of reactions. Register for the event here. Registration for undergrad and graduate students is $20, and parking is free! See the attachment and registration page for more information.

NMR Seminar with Rongfeng Zheng

MS Teams

Title: Chalcogenide-Stabilized Metal Nanoclusters: Synthesis, Characterizations, and Applications Abstract: This seminar focuses on the atomically precise gold NPs, or NCs. Au25(SR)18 was selected as a model NC to investigate their magnetic properties, with pentanethiol, hexanethiol and octanethiol used as bonding ligands. Both negatively charged and neutral NCs were synthesized, and 1H/13C NMR were used for detailed structural analysis, as well as surface bonding ligand environment analyses. The anion NC (diamagnetic) and neutral (paramagnetic) NCs are compared and by using the diamagnetic chemical shifts as references, paramagnetic Knight shifts can be calculated. These shifts measure the spin density along the carbon chain of the surface ligand. Temperature dependent NMR was used to study the spin density effect. Density functional theory calculations were used to predict the spin density on Au25(SC8H17)18 and compared with the Knight shifts observed from the experiments. New magnetic properties were observed from the Knight shifts plots. Chalcogenide stabilized NCs, such as with selenolates and tellurolates, have been less investigated, especially their exchange reactions with thiolate. The reaction mechanism, specifically the site preferences and how the mixed ligand layer is distributed on the NCs surface in the exchange reaction, is much less understood. PhSeH and (PhTe)2 were used

NJ Mass Spectrometry Discussion Group Virtual Meeting

Webex meeting

The NJ Mass Spectrometry Discussion Group is pleased to announce our February Monthly Meeting.       Speaker: Jane Gale, Ph.D., ASMS Archivist/Historian Title: Decade by Decade:  An Historical Review of Mass Spectrometry and ASMS in the Second Half of the 20th Century Abstract: Following fifteen years of meeting as part of the American Society for Testing and Materials (ASTM, now ASTM International) a small group of influential mass spectrometrists broke away from the umbrella group to found the American Society for Mass Spectrometry.  Whereas in the early days talks at annual get-togethers were dominated by topics related to the oil industry, the newly formed ASMS had a broader focus and included lively discussions of everything from mechanistic studies of molecules in the gas phase to surface science studies of materials important to the electronics industry.  The growing Society became the premier US venue in which to present both fundamental research on the technique and applied research into its use in ever-widening fields of study.  This talk will follow the Society’s growth and development over the last 70+ years, incorporating into that history the vast array of scientific developments that enabled new areas of application. Please Register below (The Meeting is Free) Meeting

Free

NMR Seminar: Structural Determination of Neurodegenerative Disease-Associated Proteins Inside Cells

MS Teams

 Abstract The misfolded proteins associated with neurodegenerative disease can adopt a variety of different conformations, some of which are toxic. Because these proteins have identical amino acid sequences, the cellular environment clearly influences the final state, yet most structural studies do not include the cellular context and, perhaps because we are not studying the correct conformation, not a single therapeutic strategy for these diseases addresses the underlying protein misfolding pathology. Using new sensitivity-enhancement technology for solid state NMR spectroscopy, Dynamic Nuclear Polarization, we study protein structure in native environments -inside living cells -to reveal how both healthy and disease-relevant cellular environments influence protein structure. Because NMR reports quantitatively, with atomic level precision, on all sampled conformation, it can not only report on structural polymorphs but also provide experimental restraints on regions of intrinsic disorder, complementing insights from cryo-electron microscopy and tomography.Using this approach, we recently demonstrated that an amyloid fibril with a solved cryo-EM structure was polymorphic and found that when those fibrils were used to seed amyloid propagation in mammalian cells, the minority polymorph in the purified setting became the majority polymorph inside cells. With this approach we can understand the mechanism of protein-based inheritance of amyloid aggregates and

Meeting of the Princeton ACS Section:“1D Lepidocrocite Titania-based Nanomaterials, Their Diverse Morphologies and Exceptional Properties”

Frick Chemistry Laboratory, Taylor Auditorium, Princeton University

Meeting of the Princeton ACS Section Tuesday, March 12, 2024 Professor Michel. W. Barsoum Drexel University, Philadelphia, PA “1D Lepidocrocite Titania-based Nanomaterials, Their Diverse Morphologies and Exceptional Properties” Frick Chemistry Laboratory, Taylor Auditorium, Princeton University Mixer (in Atrium) 6:30 pm; Lecture 7:00 pm   Abstract: Recently, we converted 15 binary and ternary titanium carbides, nitrides, borides, phosphides, and silicides into lepidocrocite-based, one dimensional, 1D, sub-nanometer nanofilaments, NFs, ≈ 5x7 Å in cross-section by reacting them with a tetramethylammonium hydroxide, TMAH, aqueous solution at ≈ 85 °C range for tens of hours. In some cases, the conversion is 100 % precluding the need for centrifuges, filters, etc. We currently routinely make 100 g batches in a lab setting. Depending on with what and the order the reaction products are washed, the 1D NFs self-assemble into loose, spaghetti-shaped fibers, ≈ 30 nm in diameter, fully inorganic TiO2 gels, pseudo 2D or porous mesoscopic particles. In all cases, the fundamental building block is 1D lepidocrocite NFs, ≈ 3 nm long, that self-assemble into the aforementioned morphologies. At this time, we believe that our materials are the only thermodynamically stable 1D NFs in water, with important implications in photo- and chemical catalysis. The production

Executive Committee Meeting

Zoom Meeting

This will be a virtual meeting held on Zoom. If you did not receive a Zoom invite, then register below and you will receive an email with the Zoom connection. Best, Sandra

Free

NJCG: Green Chromatography Webinar

NJCG is hosting an online seminar on Thursday, March 14th, 2024, focused on "Green Chromatography". Register here.  Please find the attached flyer for more information.

NMR Seminar: POKY, The Software Suite for NMR Studies and More

MS Teams

Abstract NMR spectroscopy is a powerful technique for molecular studies. In biomolecular research, it offers a wide range of unique approaches, from analyzing small compounds to investigating macromolecules, and from examining purified samples to studying complex mixtures. NMR analysis is primarily conducted in dry laboratory settings. Once the sample is prepared and inserted into the spectrometer, nearly all processes are performed using computers. When it comes to spectral analysis of biomacromolecules, such as proteins and nucleic acids, Sparky has been the gold standard program for a few decades. Donald Kneller from the Tack Kuntz group and Tom Goddard from the Tom Ferrin group were early contributors to UCSF-Sparky in the 90s. I took over from the University of California, San Francisco (UCSF) and developed NMRFAM-Sparky at the National Magnetic Resonance Facility at Madison (NMRFAM) until 2020 before I moved to the University of Colorado Denver. Since then, my group has developed the new program, POKY. POKY succeeds all the previous capabilities while provides new and enhanced features, leveraging the recent AI revolution. It is highly automated and efficient, covering assignment, peak picking, relaxation, dynamics, metabolomics, and small compound analysis. Additionally, POKY incorporates self-teaching capabilities. We have identified six different challenges,

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