Enzymes provide optimal three-dimensional structures for substrate binding and the subsequent accelerated reaction. Such folding-dependent catalytic behaviors, however, are seldom mechanistically explored with reduced structural complexity. A recent article in Nature Communications, from collaborated research between Professor Jianjun Cheng at UIUC and Professor Yao Lin at UConn, demonstrates that the α-helix, a much simpler structural motif of enzymes, can facilitate its own growth through the self-catalyzed polymerization of N-carboxyanhydride (NCA) in solvents with low dielectric constants. The leading authors with equal contributions are Ziyuan Song (UIUC), Hailin Fu (UConn) and Ryan Baumgartner (UIUC). In the paper, Hailin Fu developed a new two-stage polymerization kinetics involving a Michaelis-Menton mechanism, which helped to prove the auto-catalytic nature of the NCA polymerizations. The research was facilitated by funding from the National Science Foundation (CHE-1709820 to J.C. and DMR-1809497 to Y.L.). The editors at Nature Communications featured the article in the Editors’ Highlights of recent research on Organic Chemistry and Chemical Biology (https://www.nature.com/collections/wdzvyhgxft/content/prabhjot-saini).

Song, Z., Fu, H., Baumgartner, R., Zhu, L., Shih, K.-C., Xia, Y., Zheng, X., Yin, L., Chipot, C.*, Lin, Y.* & Cheng, J.* Enzyme-mimetic self-catalyzed polymerization of polypeptide helices. Nature Communications 10, 5470 (2019). https://www.nature.com/articles/s41467-019-13502-w