Highly Stable Pleated-Sheet Secondary Structure in Assemblies of Amphiphilic α/β-Peptides at the Air–Water Interface


  • This work was supported by the United States–Israel Binational Science Foundation (Grant No. 2005132). M.-r.L. was supported by a Korea Research Foundation Grant funded by the Korean Government (MOEHRD) (KRF-2006-214-C00053) and by the Nanoscale Science and Engineering Center at UW-Madison (NSF DMR-0425880). GIXD studies at beam-line BW1, Hasylab, DESY, were supported by the European Community-Research Infrastructure Action under the FP6 “Structuring the European Research Area” Programme (through the Integrated Infrastructure Initiative “Integrating Activity on Synchrotron and Free Electron Laser Science”).


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A nice gathering at the interface: The de novo design and characterization of amphiphilic α/β-peptides, which form ordered two-dimensional assemblies at the air–water interface composed of oligomers in pleated conformation similar to β-sheets of α-peptides, is reported. The positioning of ionic side chains along the backbone can exert a profound effect on the propensity to self-assemble.