Professor Paul Russo
School of Materials Science and Engineering, Georgia Institute of Technology
Abstract: Nature builds proteins for structure, function and reactivity, which attests to the versatility of placing different chemical groups on the same polymer backbone. Following this same design paradigm, synthetic polypeptides can mimic proteins under some circumstances. One of the more interesting functions is “gatherer”. Gatherer proteins and polypeptides can collect and even align other structures, such as colloidal silica or polymers. From a processing perspective, this function promises latex-like delivery of semiconducting polymers with greatly reduced use of environmentally unfriendly solvents. We also contemplate the polypeptide liquid crystal factory, in which interactions between colloidal particles and polypeptide mesogens assemble particles for covalent, photostimulated crosslinking.
Bio: Dr. Paul S. Russo is a Professor of Materials Science and Engineering with a joint appointment in the School of Chemistry and Biochemistry at Georgia Tech with expertise in polymer, biopolymer and particle chemistry. After obtaining a Ph.D. degree from the University of Minnesota in Chemistry in 1981, he undertook postdoctoral studies in Polymer Physics at the University of Massachusetts. His research interests are rooted in rodlike polymers, such as plant viruses, cellulose derivatives and aromatic backbone materials. Particular emphasis has been paid to molecular transport in complex fluids containing rods and to related measurement methods. He has published over 90 peer-reviewed scientific papers, and served on the editorial advisory board for Macromolecules, the ACS journal of polymers.