With the support of the Chemical Mechanism, Function, and Properties (CMFP) Program and the Chemical Catalysis Program in the Division of Chemistry, Professor Bing Gong of the State University of New York at Buffalo will be studying the function, properties, and catalytic behavior of short polyamides having spirally folded helical conformations. These slinky-like folding molecular chains, known as porous foldamers or “hollow helices”, feature an electrostatically negative, non-collapsible inner void (with a sub-nanometer diameter). These foldamers are expected to function as synthetic enzymes by accelerating chemical transformations by overcoming the energy barriers of targeted reactions within a defined pocket, similar to natural enzymes. The synthetic tunability of the hollow helices offers an adaptable structural platform for the development of enzyme-like catalysts with progressively enhanced efficiency and specificity. Broader impacts include fundamental knowledge, new catalysts, and workforce development through rigorous student training. The non-deformable inner pores of the aromatic oligoamides are strongly hydrogen-bonding and highly electronegative due to the presence of multiple inwardly oriented amide oxygen atoms. Cationic guest molecules exhibit high affinity binding to the inner pores of the hollow helices at up to 10e15/M, rivaling the tightest guest-binding systems observed in nature. This research aims to deepen our understanding of how hollow helices, wi