Investigating Peptide Structure and Polymorphism with 2D IR Spectroscopy

Event time: 
February 22, 2024 - 4:00pm to 5:00pm
SCL 160 & Livestream See map
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Join Yale Chemistry for a Silliman Physical Chemistry Seminar with Lauren Buchanan, assistant professor of chemistry, Vanderbilt University.

Lauren Buchanan is an assistant professor in the Department of Chemistry at Vanderbilt University. She is an expert in ultrafast vibrational spectroscopy and biophysical chemistry who began her independent career at Vanderbilt in 2016. A native of Oak Ridge, TN, she graduated summa cum laude from Washington University in St. Louis in 2008 with a B.A. in chemistry and mathematics.

Dr. Buchanan earned her Ph.D. with Martin T. Zanni at the University of Wisconsin–Madison in 2013. During her graduate career, she used 2D infrared spectroscopy to perform structural and mechanistic studies of several pathological amyloid proteins, including human amylin (type II diabetes), polyglutamine (Huntington’s disease), and γd-crystalline (cataracts). One of her most significant results was identifying a new prefibrillar intermediate formed by human amylin and demonstrating that fibril formation is significantly slowed when the oligomeric β-sheets of this structure are targeted by a peptide inhibitor, giving a new target for design of type II diabetes therapeutics.

After her earning her Ph.D., Dr. Buchanan was a postdoctoral researcher in the group of Richard P. Van Duyne at Northwestern University. During this time, she built the first implementation of surface-enhanced femtosecond stimulated Raman spectroscopy (SE-FSRS) using a 1 MHz laser system. As surface-enhanced Raman spectroscopy is capable of single-molecule sensitivity, the successful development of a time-resolved technique that can be applied to plasmonic systems represents a substantial step towards being able to measure single-molecule dynamics.

This seminar is generously sponsored by the Mrs. Hepsa Ely Silliman Memorial Fund.

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