ArticleACS nano2015
Ion-specific control of the self-assembly dynamics of a nanostructured protein lattice.
Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 46 citations in OpenAlex.
- Ion-Specific Effects of Alkaline Earth Metal Ion Binding to an Anionic Carboxylate Monolayer.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- SymProFold: Structural prediction of symmetrical biological assemblies.Nature communications · 2024Article
- The direct inhibitory effects of Lactobacillus acidophilus, a commensal urinary bacterium, on calcium oxalate stone development.Microbiome · 2024Article
- In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Controlled and Stable Patterning of Diverse Inorganic Nanocrystals on Crystalline Two-Dimensional Protein Arrays.Biochemistry · 2021Article
- TheMicroorganisms · 2020Review
- Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax.Nature microbiology · 2019Article
- Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly.Nature communications · 2019Article
- Article
- Functional protein nanostructures: a chemical toolbox.Chemical Society reviews · 2018Review
- Environmental Calcium Controls Alternate Physical States of the Caulobacter Surface Layer.Biophysical journal · 2017Article
- In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers.International journal of molecular sciences · 2017Article
- Analysis of self-assembly of S-layer protein slp-B53 from Lysinibacillus sphaericus.European biophysics journal : EBJ · 2017Article
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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 Ca(2+). These diagrams revealed a localized region of optimum yield of nanosheets at intermediate Ca(2+) concentration. Replacement of Mg(2+) or Ba(2+) for Ca(2+) indicates that Ca(2+) 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 Ca(2+) 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. 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.