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SUMMARY:Using Supported Lipid Bilayer Platforms to Explore the Behavior of 
 PI(4,5)P2
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20220203T160000
UID:2026-05-16-07-39-20@natsci.colostate.edu
DTSTAMP:20260516T073920
Description:About the Seminar:\n\n&nbsp\;\n\nPaul S. Cremer\, Department of
  Chemistry\, Penn State University\, University Park PA 16802\n\nPhosphati
 dylinositol 4\,5-bisphosphate\, PI(4\,5)P2 is one of the most negatively c
 harged lipids in the plasma membrane of living cells with a net charge ran
 ging from -3 to -5 near physiological pH. Its pendant phosphate groups bin
 d tightly to divalent metal cations including Ca2+ and Mg2+. Herein\, we u
 se a variety of spectroscopies and microscopies to investigate the behavio
 r of PI(4\,5)P2. For example\, it can be shown by vibrational sum frequenc
 y spectroscopy that Ca2+ has a far larger influence on the orientation of 
 the inositol ring compared to Mg2+. This is the case because Ca2+ can shed
  its inner hydration shell to bind directly to the negatively charged phos
 phate moieties and link them together. Moreover\, PI(4\,5)P2 has a strong 
 influence on interfacial water structure. Several biological mechanisms in
 volving this lipid will be discussed. These will include its role as a sec
 ond messenger as well as its ability to aid cytoskeletal attachment.\n\n\n
 \n&nbsp\;\n\nAbout the Speaker:\n\nPaul S. Cremer received his Ph.D. in Ch
 emistry in 1996 at the University of California – Berkeley. He then spen
 t two years as the Irving S. Sigal Postdoctoral Fellow at Stanford Univers
 ity before beginning his independent research career in 1998 at Texas A&am
 p\;M University\, where he became a distinguished professor and Arthur E. 
 Martell Chair of Chemistry. In early 2013\, he moved to Penn State Univers
 ity as the J. Lloyd Huck Chair in Natural Sciences where he currently hold
 s appointments in the Department of Chemistry and the Department of Bioche
 mistry and Molecular Biology. His research is at the crossroads of analyti
 cal chemistry\, physical chemistry\, biochemistry\, materials science and 
 engineering. His group has pioneered the use of linear and non-linear vibr
 ational spectroscopies to follow the interactions of ions with peptides\, 
 proteins\, lipid membranes and macromolecules. This has helped unravel the
  molecular level mechanisms of the Hofmeister series\, a rank ordering of 
 how salt ions affect physical behavior in mixtures of water\, organics\, a
 nd salts. His group has also invented a wide variety of high throughput\, 
 low sample volume microfluidic techniques. This includes temperature gradi
 ent microfluidics as well as pH modulation sensing\, a fluorescence-based 
 technique for detecting the binding of peptides\, small molecules\, ions\,
  and proteins at lipid membrane interfaces. Most recently\, his laboratory
  has pioneered the study of the metallomembrane\, including the tight bind
 ing of Cu2+ and other first row transition metal ions to lipids in bilayer
  membranes containing amine groups such as phosphatidylserine and phosphat
 idylethanolamine. 4:00 pm
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