Erich Blossey

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Professor Blossey received his baccalaureate degree was received at the Ohio State University in 1957, working on undergraduate research with Professor Michael Cava. Graduate chemistry studies were pursued with Professor Ernest Wenkert at Iowa State University (M.S. in chemistry, 1959) and with Professor Mordeaci Rubin at Carnegie Institute of Technology (nee Carnegie-Mellon University, Ph. D., 1963). Dr. Blossey received an NIH Postdoctoral Fellowship for studies with Professor Carl Djerassi at Stanford University (1962-1963) and continued his work in pharmaceutical chemistry with a postdoctoral fellowship at Syntex, S. A. in Mexico City, Mexico (1963-1964), working with Dr. Pierre Crabbe. Further studies in 1964-1965 were undertaken as a Great Lakes Colleges Association-Kettering Foundation Teaching Intern at Wabash College, working with the mentors: Professors Quentin R. Petersen and Edward Haenisch. In 1965, Dr. Blossey joined the faculty of Rollins College as an assistant professor. Since that time, he has attained the rank of Professor (1975) and held the A.G. Bush Professor of Science Chair (1981-1987) and the Donald J. and Jane M. Cram Chair of Chemistry (2002-2010) and was awarded the Arthur Vining Davis Fellowship in 1978.

Sabbatical studies included:

  • University of New Mexico as a NIH Senior Postdoctoral Fellow with Douglas Neckers with five publications and two patents; a publication example: "Polymer-Based Sensitizers for Photoöxidations. II." A. Paul Schaap, Arthur L. Thayer, Erich C. Blossey, and Douglas C. Neckers, Journal of American Chemical Society, 1975, 97, 3741-3745;
  • Oklahoma State University with Warren T. Ford resulting in four publications, an example: "Synthesis, Reactions and 13C FT-NMR Spectroscopy of Polymer Bound Steroids," E. C. Blossey, R. G. Cannon, W.T. Ford, M. Periyasamy and S. Mohanraj, Journal of Organic Chemistry, 1990, 55, 4664-4668;
  • Harvard University NSF ROA award with George M. Whitesides, resulting in a seminal publication on affinity capillary electrophoresis (ACE): “Use of Affinity Capillary Electrophoresis to Determine Kinetic and Equilibrium Constants for Binding of Arylsulfonamides To Bovine Carbonic Anhydrase” Luis Z. Avila, Yen-Ho Chu, Erich C. Blossey and George M. Whitesides, Journal of Medicinal Chemistry, 1993, 36, 126-133.

Dr. Blossey’s research interests include the area of bioorganic chemistry, utilizing polymer chemistry to develop a variety of polymer-supported reagents and reactions. Collaborative investigations with Professor Michael Doyle resulted in two publications detailing polymer-supported rhodium chiral reagents: “Preparation and Catalytic Properties of Immobilized Chiral Dirhodium (II) Carboxamidates” Michael P. Doyle, Daren J. Timmons, Jennifer S. Tumonis, Han-Mou Gau, and Erich C. Blossey, Organometallics, 2002, 21,1747-1749. “Catalysts with Mixed Ligands on Immobilized Supports. Electronic and Steric Advantages” Michael P. Doyle, Ming Yan, Han-Mou Gau, and Erich C. Blossey, Organic Letters, 2003, 5, 561-563. Recent research has focused on protein folding aided with polymer-immobilized aryl thiol reagents.

Dr. Blossey’s books include two with educational issues and advancement of active learning in the chemistry classroom: "Proceedings of the Symposium of Self-Paced Instruction in Chemistry." Edited by B.Z. Shakhashiri, Published by the Division of Chemical Education, 1974; "PSI Study Guides for Organic Chemistry," E.C. Blossey, John Wiley and Sons, Inc. 1977.

"Solutions Manual for Organic Chemistry," D.C. Neckers, M.P. Doyle and E.C. Blossey, John Wiley and Sons, 1977.

Professor Blossey holds two patents (polymeric photosensitizers), and has published a total of six books and twenty-five publications.

Blossey served as a consultant to White Laboratories, Inc. and SKB Solid Phase Peptide Synthesis Pilot Project. He was a reviewer for NSF, Research Corp., Journal of Organic Chemistry, Organic Letters, Reactive Polymers, Pearson-Prentice-Hall, McGraw-Hill, and Jones & Bartlett Publishers. He was a member of the Governing Board of Accreditation of the American College of Nurse-Midwives.


What is Happening in the Classroom?

Recent reports in print and TV have focused on the declining state of education in the U.S. This presentation will discuss changes to how educational material is disseminated in the modern classroom. Much has also been made of changes in student attitude toward learning and their use of electronic media. Is there some response by instructors that would change the picture of students sleeping through lectures and not attaining much in the way of knowledge? Educational researchers and some chemical educators have promoted what is called active learning in response to that question. The major tenet of this approach is the direct involvement of the student in the learning process. It is not acceptable to have a student sitting through a lecture like a “bump-on-a-log”. A major method for actively engaging students is through small problem-solving groups and frequent assessment of what ever takes place in and outside the classroom. The device that makes the assessment straightforward for the instructor and class is the clicker. The talk will detail how the small problem-solving groups and the clickers’ work. Research studies that indicate improved performance over lecture methods. References: Eric Mazur Peer Instruction: A User’s Manual, Prentice-Hall, Upper Saddle River, NJ, 1997. Donald R. Paulson Active learning and cooperative learning in the organic chemistry lecture class, J. Chem. Ed. 1999, 76, 1136-1140. J. R. MacArthur & L. L. Jones A review of literature reports of clickers applicable to college chemistry classrooms, Chemistry Education Research & Practice, 2008, 9, 187-195.

Protein Folding and Alzheimer’s and Other Neurodegenerative Diseases: What Is The Connection?

There is some connection between how proteins fold and a many neurodegenerative diseases like Alzheimer’s. This talk will examine neurodegenerative diseases that have a protein folding “problem”, these include: Alzheimer’s, (AD) Parkinson’s (PD), Huntington’s, transmissible encephalopthies (Mad Cow disease or kuru, scrapie, Creutzfeld-Jacob, etc.), Gerstmann-Straussler-Scheinker syndrome, Down’s syndrome, total familial insomnia, amyotrophic lateral sclerosis (Lou Gehrig’s disease), diabetes mellitus (Type II diabetes), and cataracts (misfolded -crystallin). Besides having misfolded proteins, most have another common problem, the decisive agent or cause is not known with certainty. AD and PD affect over 9 million persons in the U. S. alone, with over 50% contracting AD after age 70. The diseases share a common outcome: the accumulation of aggregated proteins. However recent studies of AD indicate that misfolding of proteins results in small multiple units of protein, like dimers, etc, that lead to a cascade of oxidative reactions (ROS, reactive oxygen system) that destroy neurons in the brain and hence death in the individual. The exact toxic nature of various intermediates and how they destroy neurons is not known at this time. Without the “smoking gun”, it is difficult to produce a “magic” pill or curative procedure and treatment. A “layman’s” version of what takes place in protein folding, how this folding process may result in misfolded proteins, and some of the strategies for the prevention of neurodegeneration will be discussed.


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