Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice

Rad, Behzad; Haxton, Thomas K.; Shon, Albert; Shin, Seong-Ho; Whitelam, Stephen; Ajo-Franklin, Caroline M.

doi:10.1021/nn502992x

Title: Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice

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Abstract

Self-assembling proteins offer a potential means of creating nanostructures with complex structure and function. However, using self-assembly to create nanostructures with long-range order whose size is tunable is challenging, because the kinetics and thermodynamics of protein interactions depend sensitively on solution conditions. Here we systematically investigate the impact of varying solution conditions on the self-assembly of SbpA, a surface-layer protein from Lysinibacillus sphaericus that forms two-dimensional nanosheets. Using high-throughput light scattering measurements, we mapped out diagrams that reveal the relative yield of self-assembly of nanosheets over a wide range of concentrations of SbpA and Ca²⁺. These diagrams revealed a localized region of optimum yield of nanosheets at intermediate Ca²⁺ concentration. Replacement of Mg²⁺ or Ba²⁺ for Ca²⁺ indicates that Ca²⁺ acts both as a specific ion that is required to induce self-assembly and as a general divalent cation. In addition, we use competitive titration experiments to find that 5 Ca²⁺ bind to SbpA with an affinity of 67.1 ± 0.3 μM. Finally, we show via modeling that nanosheet assembly occurs by growth from a negligibly small critical nucleus. We also chart the dynamics of nanosheet size over a variety of conditions. In conclusion, our results demonstrate control of the dynamicsmore »« less

Authors:

Rad, Behzad; Haxton, Thomas K.; Shon, Albert ^[1]; Shin, Seong-Ho ^[2]; Whitelam, Stephen; Ajo-Franklin, Caroline M.

Department of Chemical and Biomolecular Engineering, UC Berkeley, Berkeley, California 94720-1462, United States
Department of Chemistry, UC Berkeley, Berkeley, California 94720-1460, United States

Publication Date:: Wed Dec 17 00:00:00 EST 2014

Research Org.:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Org.:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

OSTI Identifier:: 1168700

Alternate Identifier(s):: OSTI ID: 1257359

Grant/Contract Number:: AC02-05CH11231; R01GM105404

Resource Type:: Published Article

Journal Name:: ACS Nano

Additional Journal Information:: Journal Name: ACS Nano Journal Volume: 9 Journal Issue: 1; Journal ID: ISSN 1936-0851

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: English

Subject:: 77 NANOSCIENCE AND NANOTECHNOLOGY; protein interactions; biomaterials; nanostructures; self-assembly dynamics; Ca2+ binding

Citation Formats


                    Rad, Behzad, Haxton, Thomas K., Shon, Albert, Shin, Seong-Ho, Whitelam, Stephen, and Ajo-Franklin, Caroline M. Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice.  United States: N. p., 2014. 
Web.  doi:10.1021/nn502992x.

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                    Rad, Behzad, Haxton, Thomas K., Shon, Albert, Shin, Seong-Ho, Whitelam, Stephen, & Ajo-Franklin, Caroline M. Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice.  United States.  https://doi.org/10.1021/nn502992x

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                    Rad, Behzad, Haxton, Thomas K., Shon, Albert, Shin, Seong-Ho, Whitelam, Stephen, and Ajo-Franklin, Caroline M. Wed .  
"Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice".  United States.  https://doi.org/10.1021/nn502992x.

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@article{osti_1168700,

  title        = {Ion-Specific Control of the Self-Assembly Dynamics of a Nanostructured Protein Lattice},

  author       = {Rad, Behzad and Haxton, Thomas K. and Shon, Albert and Shin, Seong-Ho and Whitelam, Stephen and Ajo-Franklin, Caroline M.},

  abstractNote = {Self-assembling proteins offer a potential means of creating nanostructures with complex structure and function. However, using self-assembly to create nanostructures with long-range order whose size is tunable is challenging, because the kinetics and thermodynamics of protein interactions depend sensitively on solution conditions. Here we systematically investigate the impact of varying solution conditions on the self-assembly of SbpA, a surface-layer protein from Lysinibacillus sphaericus that forms two-dimensional nanosheets. Using high-throughput light scattering measurements, we mapped out diagrams that reveal the relative yield of self-assembly of nanosheets over a wide range of concentrations of SbpA and Ca2+. These diagrams revealed a localized region of optimum yield of nanosheets at intermediate Ca2+ concentration. Replacement of Mg2+ or Ba2+ for Ca2+ indicates that Ca2+ acts both as a specific ion that is required to induce self-assembly and as a general divalent cation. In addition, we use competitive titration experiments to find that 5 Ca2+ bind to SbpA with an affinity of 67.1 ± 0.3 μM. Finally, we show via modeling that nanosheet assembly occurs by growth from a negligibly small critical nucleus. We also chart the dynamics of nanosheet size over a variety of conditions. In conclusion, our results demonstrate control of the dynamics and size of the self-assembly of a nanostructured lattice, the constituents of which are one of a class of building blocks able to form novel hybrid nanomaterials.},

  doi          = {10.1021/nn502992x},

  journal      = {ACS Nano},

  number       = 1,

  volume       = 9,

  place        = {United States},

  year         = {Wed Dec 17 00:00:00 EST 2014},

  month        = {Wed Dec 17 00:00:00 EST 2014}

}

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