January Monthly Meeting

WHEN: Wednesday, January 8, 2020
WHERE: Duquesne University
RSVP BY: Thursday, January 2, 2020 by NOON
Dinner reservations are no longer being accepted.

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    5:30 PM Social Hour: Shepperson Suite
    5:30 PM SSP Technology Forum: Power Center Ballroom
    6:30 PM Dinner: Power Center Ballroom
    Student Affiliate Meeting: Shepperson Suite
    7:15 PM Business Meeting: Power Center Ballroom
    7:45 PM Technical Program: Power Center Ballroom


    Please note change in venue.
    5:30 PM Technology Forum: Room 613 (Duquesne Union)
    5:30 PM Social Hour: Africa Room (Duquesne Union)
    6:30 PM Dinner: Africa Room (Duquesne Union)
    7:45 PM Business Meeting: Africa Room (Duquesne Union)
    8:00 PM Technical Program: Africa Room (Duquesne Union)
    Student Affiliate Meeting: Shepperson Suite


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Ryan O’Shea, Founder & Host of Future Grind

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“Sensing the Future – Combining Wearables, Al, & loT”
Decreasing size, increasing capabilities, and diminishing costs mean that sensors are becoming ubiquitous. They are in our homes, cars, offices, electronics, and even on and sometimes in our bodies. All of these sensors are generating data, and this data needs to be analyzed to identify valuable information and actionable insights. The sheer amount of data, however, makes this a daunting and often impossible task for humans. At a certain scale, the best method of making sense of this data is leveraging the capabilities of machine learning. Because of this, the futures of sensors, Internet of Things devices, and artificial intelligence are largely interconnected and interrelated – the future success of one is largely dependent on the future success of the others.

This high-level, largely non-technical presentation will provide an overview on how sensors are being used today, their relationship with Internet of Things (IoT) devices, and how machine learning and artificial intelligence are being used to analyze the data they generate. We’ll also explore the future applications and implications of these sensors, as well as the rise of smart watches, smart clothing, smart tattoos, and implantable devices. Beyond this, we’ll identify and discuss some of the ethical, societal, and regulatory concerns around issues of data privacy and security, bodily autonomy, “medicine”, citizen science, and more.

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Dr. Lisa Holland, Professor of Chemistry, C. Eugene Bennett Department of Chemistry, West Virginia University

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“Designer Separations with Smart Nanomaterials”
Capillary electrophoresis separations play an important role in challenging bioanalyses. With new materials and strategies, this separation technique is prominent in next generation therapeutics and in shedding light on physiological systems. This presentation will reveal the role of biocompatible nanomaterials and instrumental advances to leverage the high efficiency and throughput of capillary separations. Advances in this technology overcome barriers to universally analyzing proteins, which are among the most diverse class of physiologically relevant biomolecules. In particular, protein isoforms and post-translational modifications will be addressed. A rapid, inexpensive, and automated method is demonstrated to successfully quantify modifications with N-glycans (e.g. fucosylation, sialylation, branching, and bisection), which are a result of both normal and aberrant physiological processes. With this advance subtle differences in proteins can be distinguished. The separation is facilitated with self-assembled nanogels in a capillary that also contains stationary zones of lectins and/or enzymes. The nanogel electrophoresis generates separation efficiencies of 500,000 plates and easily resolves positional isomers. Because this technology is biocompatible, native analyses are also feasible. The nanomaterial additives used for these separations have a thermally dependent viscosity, which provides a means to precisely control and position specific zones of enzymes and lectins within the capillary to both process and separate proteins in nanoliter volumes in an automated instrument. The nanogel supports successive reaction in a channel (i.e. in series) because the viscosity of nanophases minimizes dispersion. Each molecular affinity step of the analysis utilizes a small (~5 nL) re in the channel. Nanogel preparations are inexpensive, costing $0.09 for 5 L. The structural features of proteins are identified and quantified without the need for standards. Moreover, the nanophases are compatible with UV absorbance, fluorescence, and mass spectrometry detection. Cost-effective and rapid monitoring of glycosylation is critical to ensuring the efficacy of protein-based antibody drugs and to elucidating the role of N-glycans in physiological processes.