A Triply Templated Artificial β-Sheet

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Abstract
This paper describes the design, synthesis, and structural evaluation of a compound (4) comprising three molecular templates and a peptide strand that mimics a three-stranded protein β-sheet. Two of the templates mimic the hydrogen-bonding functionality of peptide β-strands and serve as the top and bottom strands by embracing the peptide strand, which is located in the middle of the sheet. The remaining template holds the three strands next to each other. The synthesis of artificial β-sheet 4 begins with the bottom template and involves the sequential addition of the middle and top strands. 1H NMR chemical shift and NOE studies establish that this compound folds to adopt a hydrogen-bonded β-sheetlike structure in CDCl3 solution. Chemical shift studies indicate that triply stranded artificial β-sheet 4 is more tightly folded than its smaller doubly stranded homologue, artificial β-sheet 1.