Effects of Surface Ligand Density on Lipid-Monolayer-mediated 2D Assembly of Proteins

Fukuto, M; Wang, S; Lohr, M; Kewalramani, S; Yang, L

doi:10.1039/b917139h

Title: Effects of Surface Ligand Density on Lipid-Monolayer-mediated 2D Assembly of Proteins

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Abstract

The two-dimensional (2D) assembly of the protein streptavidin on a biotin-bearing lipid monolayer was studied as a function of the surface density of biotin, a protein-binding ligand, by means of in situ X-ray scattering and optical Brewster angle microscopy measurements at the liquid-vapor interface. Although this model system has been studied extensively, the relationship between the surface biotin density and the adsorption, 2D phase behavior, and binding state of streptavidin has yet to be determined quantitatively. The observed equilibrium phase behavior provides direct structural evidence that the 2D crystallization of the lipid-bound streptavidin occurs as a density-driven first-order phase transition. The minimum biotin density required for the 2D crystallization of streptavidin is found to be remarkably close to the density of the ligand-binding sites in the protein crystal. Moreover, both above and below this transition, the observed biotin-density dependence of protein adsorption is well described by the binding of biotin-bearing lipids at both of the two available sites per streptavidin molecule. These results imply that even in the low-density noncrystalline phase, the bound proteins share a common, fixed orientation relative to the surface normal, and that the 2D crystallization occurs when the lateral protein density reaches 50-70% of the 2Dmore »« less

Authors:: Fukuto, M; Wang, S; Lohr, M; Kewalramani, S; Yang, L

Publication Date:: Fri Jan 01 00:00:00 EST 2010

Research Org.:: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source

Sponsoring Org.:: DOE - OFFICE OF SCIENCE

OSTI Identifier:: 1020171

Report Number(s):: BNL-96021-2011-JA
Journal ID: ISSN 1744-683X; TRN: US201116%%151

DOE Contract Number:: DE-AC02-98CH10886

Resource Type:: Journal Article

Journal Name:: Soft Matter

Additional Journal Information:: Journal Volume: 6; Journal Issue: 7; Journal ID: ISSN 1744-683X

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; ADSORPTION; BIOTIN; CRYSTALLIZATION; LIPIDS; MICROSCOPY; ORIENTATION; PROTEINS; SCATTERING; national synchrotron light source

Citation Formats


                    Fukuto, M, Wang, S, Lohr, M, Kewalramani, S, and Yang, L. Effects of Surface Ligand Density on Lipid-Monolayer-mediated 2D Assembly of Proteins.  United States: N. p., 2010. 
        Web.  doi:10.1039/b917139h.

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                    Fukuto, M, Wang, S, Lohr, M, Kewalramani, S, & Yang, L. Effects of Surface Ligand Density on Lipid-Monolayer-mediated 2D Assembly of Proteins.  United States.  https://doi.org/10.1039/b917139h

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                    Fukuto, M, Wang, S, Lohr, M, Kewalramani, S, and Yang, L. 2010.  
        "Effects of Surface Ligand Density on Lipid-Monolayer-mediated 2D Assembly of Proteins".  United States.  https://doi.org/10.1039/b917139h.

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@article{osti_1020171,

  title        = {Effects of Surface Ligand Density on Lipid-Monolayer-mediated 2D Assembly of Proteins},

  author       = {Fukuto, M and Wang, S and Lohr, M and Kewalramani, S and Yang, L},

  abstractNote = {The two-dimensional (2D) assembly of the protein streptavidin on a biotin-bearing lipid monolayer was studied as a function of the surface density of biotin, a protein-binding ligand, by means of in situ X-ray scattering and optical Brewster angle microscopy measurements at the liquid-vapor interface. Although this model system has been studied extensively, the relationship between the surface biotin density and the adsorption, 2D phase behavior, and binding state of streptavidin has yet to be determined quantitatively. The observed equilibrium phase behavior provides direct structural evidence that the 2D crystallization of the lipid-bound streptavidin occurs as a density-driven first-order phase transition. The minimum biotin density required for the 2D crystallization of streptavidin is found to be remarkably close to the density of the ligand-binding sites in the protein crystal. Moreover, both above and below this transition, the observed biotin-density dependence of protein adsorption is well described by the binding of biotin-bearing lipids at both of the two available sites per streptavidin molecule. These results imply that even in the low-density noncrystalline phase, the bound proteins share a common, fixed orientation relative to the surface normal, and that the 2D crystallization occurs when the lateral protein density reaches 50-70% of the 2D crystal density. This study demonstrates that in addition to a well-defined molecular orientation, high lateral packing density is essential to the 2D crystallization of proteins.},

  doi          = {10.1039/b917139h},

  url          = {https://www.osti.gov/biblio/1020171},
  journal      = {Soft Matter},

  issn         = {1744-683X},

  number       = 7,

  volume       = 6,

  place        = {United States},

  year         = {Fri Jan 01 00:00:00 EST 2010},

  month        = {Fri Jan 01 00:00:00 EST 2010}

}

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