Free floating Ultra-Thin Two-Dimensional Crystals From Sequence-Specific Peptoid Polymers (Ki Tae Nam, Sarah A. Selby, Philip H. Choi, Amanda B. Marciel, Ritchie Chen, Li Tan, Tammy K. Chu, Ryan A. Mesch, Byoung-Chul Lee, Michael D. Connolly, Christian Kisielowski and Ronald Zuckermann)

Peptoids are sequence specific, oligo-N-substituted glycine polymers designed to mimic the structure and functionality of proteins. Mixing a 1:1 ratio of two oppositely charged peptoid 36mers of a specific sequence in aqueous solution results in the formation of giant, free-floating sheets with only 2.7 nm thickness. Direct visualization of aligned individual peptoid chains in the sheet structure was achieved using aberration-corrected transmission electron microscopy. Specific binding of a protein to ligand-functionalized sheets was also demonstrated. The synthetic flexibility and biocompatibility of peptoids provide a flexible and robust platform for integrating functionality into defined two-dimensional nanostructures.

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