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”).
Communication
Highly Stable Pleated-Sheet Secondary Structure in Assemblies of Amphiphilic α/β-Peptides at the Air–Water Interface†
Article first published online: 18 DEC 2009
DOI: 10.1002/anie.200904566
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Segman, S., Lee, M.-r., Vaiser, V., Gellman, Samuel H. and Rapaport, H. (2010), Highly Stable Pleated-Sheet Secondary Structure in Assemblies of Amphiphilic α/β-Peptides at the Air–Water Interface. Angew. Chem. Int. Ed., 49: 716–719. doi: 10.1002/anie.200904566
- †
Publication History
- Issue published online: 13 JAN 2010
- Article first published online: 18 DEC 2009
- Manuscript Received: 16 AUG 2009
Funded by
- United States–Israel Binational Science Foundation. Grant Number: 2005132
- Korean Government (MOEHRD). Grant Number: KRF-2006-214-C00053
- Nanoscale Science and Engineering Center at UW-Madison. Grant Number: NSF DMR-0425880
Keywords:
- β-sheet;
- foldamers;
- monolayers;
- peptides;
- self-assembly

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.

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