Two-dimensional crystallization of proteins on lipid monolayers at the air–water interface and transfer to an electron microscopy grid

Brisson, Alain; Bergsma-Schutter, Wilma; Oling, Frank; Lambert, Olivier; Reviakine, Ilya

doi:10.1016/s0022-0248(98)00834-3

Cited by 65 publications

(65 citation statements)

References 34 publications

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“…29. Briefly, a lipid monolayer was formed by applying 0.6 l of a lipid mixture containing 250 M DOPC and 125 M DOPS dissolved in chloroform:hexane ͑1:1, v/v͒ over a 17 L droplet of 25 g / mL Anx5-peptide in buffer C. After 1 h incubation necessary for crystallization, the material present at the air-water interface was transferred onto a perforated carbon-coated 200-mesh copper EM grid by horizontal lifting.…”

Section: J Transmission Electron Microscopymentioning

confidence: 99%

“…29,30,[33][34][35] 1. Characterization of the binding of Anx5-peptide complexes to SLBs, by QCM-D Figure 2 presents the QCM-D adsorption responses obtained with both Anx5-RGD and Anx5-IKVAV, as well as with Anx5, on SLBs.…”

Section: B Binding and Organization Of Anx5-peptide 2d Matrices On Slbsmentioning

confidence: 99%

“…Two-dimensional crystals of Anx5-RGD were obtained in the same conditions as for Anx5. 29,33 Figure 3͑C͒ presents a 2D projection map of an Anx5-RGD 2D crystal, calculated by Fourier analysis at 2.5 nm resolution. The 2D crystals of Anx5-RGD are made of trimers arranged with p6 symmetry ͑unit cell dimensions: a = b = 17.7 nm, ␥ = 120°͒, as Anx5 2D crystals.…”

Section: Characterization Of the 2d Organization Of Anx5-peptide Matrmentioning

confidence: 99%

“…The basic concept was to exploit the property presented by several proteins of self-assembling in 2D matrices on a lipid surface. [28][29][30] The main potential advantages of this mode of peptide presentation are the control of the orientation and of the density of peptides. In addition, this system allows addressing questions of interest in cell adhesion, such as the influence of the mobility of the ligands, by comparing the behavior of immobile protein-peptides with mobile lipopeptides on SLBs.…”

Section: Introductionmentioning

confidence: 99%

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Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: An efficient platform for cell adhesion

et al. 2007

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Understanding and controlling cell adhesion to biomaterials and synthetic materials are important issues in basic research and applied sciences. Supported lipid bilayers ͑SLBs͒ functionalized with cell adhesion peptides linked to lipid molecules are popular platforms of cell adhesion. In this paper, an alternative approach of peptide presentation is presented in which peptides are stereo-selectively linked to proteins self-assembling in a rigid two-dimensional ͑2D͒ matrix on SLBs. Annexin-A5 ͑Anx5͒ was used as prototype protein for its known properties of forming stable and rigid 2D matrices on lipid surfaces. Two types of Anx5-peptide complexes, containing either a RGD or an IKVAV sequence, were synthesized. The authors show that both Anx5-peptide complexes present the same properties of binding and 2D organization on lipid surfaces as Anx5, when investigated by quartz crystal microbalance with dissipation monitoring, atomic force microscopy, and transmission electron microscopy techniques. Anx5-RGD and Anx5-IKVAV 2D matrices were found to promote specific adhesion of human saphenous vein endothelial cells and mouse embryonic stem cells, respectively. The influence of the surface density of exposed peptides on cell adhesion was investigated, showing that cells attach to Anx5-peptide matrices when the average distance between peptides is smaller than about 60 nm. This cell adhesion platform provides control of the orientation and density of cell ligands, opening interesting possibilities for future applications.

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Section: J Transmission Electron Microscopymentioning

confidence: 99%

Section: B Binding and Organization Of Anx5-peptide 2d Matrices On Slbsmentioning

confidence: 99%

Section: Characterization Of the 2d Organization Of Anx5-peptide Matrmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: An efficient platform for cell adhesion

et al. 2007

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“…This is helpful because the eye averages when their images are examined, and otherwise minor features become evident. In addition, the underlying periodicity makes possible application of Fourier filtering and averaging processes that can yield improved images (Brisson et al, 1999;Kuznetsov et al, 1997). AFM may, in the best of cases, yield lattice resolution images of crystals that even reveal some gross features of the macromolecules in the unit cells.…”

Section: Sample Preparation and Data Acquisitionmentioning

confidence: 99%

Macromolecular crystal growth as revealed by atomic force microscopy

McPherson

Kuznetsov

Malkin

et al. 2003

Journal of Structural Biology

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Direct visualization of macromolecular crystal growth using atomic force microscopy (AFM) has provided a powerful tool in the delineation of mechanisms and the kinetics of the growth process. It has further allowed us to evaluate the wide variety of impurities that are incorporated into crystals of proteins, nucleic acids, and viruses. We can, using AFM, image the defects and imperfections that afflict these crystals, the impurity layers that poison their surfaces, and the consequences of various factors on morphological development. All of these can be recorded under normal growth conditions, in native mother liquors, over time intervals ranging from minutes to days, and at the molecular level.

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Simulation of two‐dimensional streptavidin crystallization

2001

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We present lattice Monte Carlo simulations of the growth of streptavidin islands at a biotinylated lipid layer. The model employed takes into account attractive anisotropic lateral interactions between streptavidin tetramers. With a minimal set of interactions, we reproduce the formation of rectangular islands experimentally observed at pH > or = 9.0. Specifically, we analyze two scenarios of the island growth. First, if streptavidin is rapidly adsorbed at t = 0 (stepwise coverage change without ongoing adsorption), the average linear island size is found to grow according to the Lifshitz-Slyozov law, R proportional to t(1/3). Second, if the island growth occurs in parallel with streptavidin adsorption limited by diffusion in the solution, the Lifshitz-Slyozov law is also applicable, but only at the late stage, when the streptavidin coverage is appreciable.

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Two-dimensional crystallization of proteins on lipid monolayers at the air–water interface and transfer to an electron microscopy grid

Cited by 65 publications

References 34 publications

Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: An efficient platform for cell adhesion

Peptide-presenting two-dimensional protein matrix on supported lipid bilayers: An efficient platform for cell adhesion

Macromolecular crystal growth as revealed by atomic force microscopy

Simulation of two‐dimensional streptavidin crystallization

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