Samuel H. Gellman is the Ralph F. Hirschmann Professor of Chemistry (also Irving Shain Chair and Vilas Research Professor) at the University of Wisconsin–Madison, where he has been a faculty member since 1987. He is a leading organic chemist and chemical biologist specializing in peptide and protein mimicry, foldamers, and the design of synthetic molecules that mimic biopolymer structures and functions. His pioneering research on foldamers—unnatural oligomers that adopt stable folded conformations—has provided fundamental insights into protein folding, molecular recognition, and applications in chemical biology and therapeutics. Gellman has authored over 400 publications, with citations exceeding 53,000. His honors include election to the National Academy of Sciences and the American Academy of Arts and Sciences, plus ACS awards such as the Ralph F. Hirschmann Award in Peptide Chemistry (2007) and the Ronald Breslow Award in Biomimetic Chemistry (2014), alongside the Vincent du Vigneaud Award from the American Peptide Society. He earned his bachelor’s from Harvard University, Ph.D. from Columbia University, and completed postdoctoral studies at Caltech.

2026 CME NASA Symposium Abstract – Foldamers: Extrapolating from Proteins

Folded biopolymers perform diverse functions in biological systems. Most of these operations require the biopolymer chain to adopt a specific conformation. Over the past three decades there has been growing interest in the prospect that biopolymer functions might be recapitulated and perhaps even improved upon with unnatural oligomers that manifest discrete folding preferences. Such systems are referred to generically as “foldamers”. This lecture will introduce the goals of this field, and survey progress toward those goals we have achieved with peptidic oligomers that contain β-amino acid residues or other non-proteinogenic subunits, exclusively or in combination with α-amino acid residues. Recent developments with foldamers for catalytic or biological applications will be presented.