February 29 – March 4, 2016

Monday, February 29

Psychology Student Presentations
Interim in Inda
4:00 pm, RNS 210

MSCS Colloquium – Design considerations and alternatives for clinical trials of medical devices
Ted Lystig ’93 Director, Corporate Biostatistics at Medtronic
A recent high-profile series of hypertension trials provides an intriguing setting for a conversation around trial design issues for medical devices.  I will provide an overview of the therapy area and published trials, and then move to a discussion of various study options that were considered as subsequent candidate trials.  I’ll then discuss the operational properties of the designs, and talk about why they matter.  The presentation as a whole helps to illustrate how quantitative training can better prepare you to contribute in important, sometimes unexpected ways as a working professional.  Coursework in statistics is not necessary to follow the talk, but would allow you to appreciate more of the details.
3:15pm Cookies and Conversation; 3:30-4:30 P.M., RNS 310

Tuesday, March 1

Seminar: RNS 150 7pm

StoMols Speaker

Wednesday, March 2

Physics Colloquium 
Neutron Stars as a Laboratory
Demian Cho, Assistant Professor of Physics, St. Mary’s University-Winona, Minnesota
2:00 pm, RNS 210

Thursday, March 3

Seminar: Title
Speaker name and title
Time, Room

Friday, March 4

Chemistry Seminar: Designing peptides with non-natural residues to inhibit therapeutically-relevant protein-protein interactions
James Checco, ’10 Alumni

Peptides that bind specifically to protein surfaces can be useful as mediators of therapeutically-relevant protein-protein interactions or as diagnostic tools for disease marker detection. However, conventional peptides, comprised exclusively of the 20 proteinogenic α-amino acid residues (“α-peptides”), are rapidly degraded in biological systems by protease enzymes. The low half-life of α-peptides in vivo significantly limits the scope of their therapeutic use. Backbone-modified peptides that contain a mixture of α-residues and non-natural β-residues (which contain two carbon atoms in their backbone) can effectively mimic the structure and function of natural peptides. Such “α/β-peptides” can show high affinity and selectivity for target proteins and are less susceptible to proteolytic degradation than are α-peptides. This research develops a general strategy to design α/β-peptides that selectively target diverse and topologically-complex protein surfaces, such as the receptor-binding surface of vascular endothelial growth factor (VEGF), a mediator of angiogenesis that plays a major role in several diseases.

3:00 Refreshments, 3:15 Seminar, RNS390