Welcome to the Georgia Institute of Technology - Parker H. Petit Institute for Bioengineering and Bioscience (IBB)
This year the Suddath Symposium is aimed at "Prions and Protein Misfolding," and organized in conjuction with the Center for Nanobiology of the Macromolecular Assembly Disorders (NanoMAD) at Georgia Tech.
Each year the Petit Institute for Bioengineering and Bioscience at Georgia Tech hosts the Suddath Symposium to honor Leroy "Bud" Suddath, PhD, a late professor of the School of Chemistry and Biochemistry. Suddath helped determine the structure of tRNA while a postdoctoral associate in the laboratory of Alexander Rich, PhD, MIT. The Suddath Symposium changes topic each year, attracting leaders in varying fields in biological sciences.
A variety of human diseases, such as Alzheimer, Parkinson, or Huntington diseases, amyotrophic lateral sclerosis, possibly type II diabetes and others, are caused by self-assembled highly ordered aggregates of misfolded proteins (amyloids and neural inclusions) and represent a serious challenge to health care. Many of these diseases are fatal, most are incurable and some are age-dependent, so that their impact will only grow with the eradication of other diseases and an increase in human life span. Infectious amyloids (prions) cause transmissible encephalopathies (such as "mad cow" disease) and may spread, for example from domestic animals to humans consuming infected meat. At least some other amyloids are also transmissible at cellular level. Studies of prion proteins in lower eukaryotes such as yeast have demonstrated that amyloid disorders originate from malfunctioning of the evolutionarily conserved mechanisms, governing the assembly of multi-molecular structures and contributing to epigenetic transfer of heritable information. Some amyloids play biologically positive roles and/or have technological applications. Amyloid is proposed to be an ancient protein fold potentially involved in emergence of structures in prebiotic world. Studies of prions and other aggregates of misfolded proteins are important for both finding long-term solutions for amyloid disorders and understanding the molecular basis of protein evolution.
The 2012 Suddath Symposium is organized by Yury Chernoff, PhD, Professor of Biology at Georgia Tech, and Director of Center for NanoMAD, with assistance from Center for NanoMAD members. Program was composed by Dr. Chernoff and Center for NanoMAD Committee, that includes Andreas Bommarius, PhD, Professor of Chemical and Biomolecular Engineering at Georgia Tech, and David Lynn, PhD, Professor of Chemistry and Biology at Emory University. The meeting received financial support from the Parker H. Petit Institute for Bioengineering and Bioscience, with a contribution from Center for NanoMAD.
Since its inception in 1995, IBB has been the driving force of the biotechnology community at Georgia Tech and has been an exemplary model for other campuses across the nation. 