Two-dimensional ordered β-sheet lipopeptide monolayers

被引：0

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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Journal article (JA)

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页码：13959 / 13966