Researchers have learned to control the “handedness” of peptoids, a crucial factor in precision drug delivery and diagnostics.
Nature is filled with extraordinarily precise molecular shapes that fit together like a hand in glove. Proteins, for example, can assemble into a wide variety of well-defined shapes that grant them their function.
“Depending on their shape, proteins can fit together with other proteins to perform functions or malfunction by clumping together, as observed in
For this experiment, Chen and his team chose to pursue corkscrew-like helical structures because of their biological importance. In fact, most proteins contain these basic helical structures.
Previous peptoid synthesis methods would yield a mix of left- and right-handed helices. In nature, proteins need to be in a specific conformation to perform their functions—most being left-handed.
“Other groups before us were able to synthesize peptoid nanohelices, but precisely controlling their shapes and handedness remained a challenge,” said Chen. “Being able to control their shapes would not only open the door for designing future materials, it would also provide insights into biological processes involving these structures.”
Using a combination of experimental and computational techniques, Chen and his team discovered a way to control the handedness of a peptoid helix. Similar to proteins, peptoids are created from amino DOI: 10.1038/s41467-024-46839-y
“Hierarchical Self-Assembly of Multidimensional Functional Materials from Sequence-Defined Peptoids” by Li Shao, Dehong Hu, Shao-Liang Zheng, Thi Kim Hoang Trinh, Wenhao Zhou, Haoyu Wang, Yanxu Zong, Changning Li and Chun-Long Chen, 24 April 2024, Angewandte Chemie International Edition.
DOI: 10.1002/anie.202403263
Both studies were primarily supported by the Department of Energy, Office of Science, Basic Energy Sciences program as part of the Energy Frontier Research Centers program: CSSAS – The Center for the Science of Synthesis Across Scales.