Samuel H. Gellman Research Group

University of Wisconsin-Madison

Can systematic backbone modification of polypeptides produce stable molecules that retain target-binding while resisting proteolysis? The group synthesizes α/β-peptides to test how backbone extension alters folding and recognition by partner proteins. Researchers use chemical synthesis and crystallography to characterize α/β-peptide helices bound to protein targets such as an engineered gp41 fragment. The lab measures biological stability and protease resistance to assess persistence of modified polypeptides in cellular assays. They investigate backbone-modified agonists for B-family GPCRs to map how modifications change receptor signaling profiles.