Two-dimensional ordered β-sheet lipopeptide monolayers

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作者：
Cavalli, Silvia [1 ]
Handgraaf, Jan-Willem [1 ]
Tellers, Emily E. [1 ]
Popescu, Daniela C. [2 ]
Overhand, Mark [1 ]
Kjaer, Kristian [3 ]
Vaiser, Vladimir [4 ]
Sommerdijk, Nico A. J. M. [2 ]
Rapaport, Hanna [4 ]
Kros, Alexander [1 ]
机构：
[1] Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
[2] Laboratory of Macromolecular and Organic Chemistry, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven, Netherlands
[3] Niels Bohr Institute, University of Copenhagen, DK-2100 Copenhagen, Denmark
[4] Department of Biotechnology Engineering, Ben Gurion University of the Negev, P.O. Box 653, 84105, Beer-Sheva, Israel
来源：
Journal of the American Chemical Society | 2006年 / 128卷 / 42期
关键词：
A series of amphiphilic lipopeptides; ALPs; consisting of an alternating hydrophilic and hydrophobic amino acid residue sequence coupled to a phospholipid tail; was designed to form supramolecular assemblies composed of β-sheet monolayers decorated by lipid tails at the air-water interface. A straightforward synthetic approach based on solid-phase synthesis; followed by an efficient purification protocol was used to prepare the lipid-peptide conjugates. Structural insight into the organization of monolayers was provided by surface pressure versus area isotherms; circular dichroism; Fourier transform infrared spectroscopy; and Brewster angle microscopy. In situ grazing-incidence X-ray diffraction (GIXD) revealed that lipopeptides six to eight amino acids in length form a new type of 2D self-organized monolayers that exhibit β-sheet ribbons segregated by lipid tails. The conclusions drawn from the experimental findings were supported by a representative model based on molecular dynamics simulations of amphiphilic lipopeptides at the vacuum-water interface. © 2006 American Chemical Society;
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页码：13959 / 13966
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