Controlling Protein Nanocage Assembly with Hydrostatic Pressure
| Autor: | Adam W. Perriman, Ben M. Carter, Andrew J. Smith, Helmut Cölfen, Valeska P. Ting, Kristian Le Vay, T.-Y. Dora Tang, Robert P. Rambo, Daniel W. Watkins, J. L. Ross Anderson |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Circular dichroism
Protein subunit Dimer Hydrostatic pressure Kinetics BrisSynBio 010402 general chemistry 01 natural sciences Biochemistry Catalysis chemistry.chemical_compound Colloid and Surface Chemistry Bacterial Proteins X-Ray Diffraction Scattering Small Angle Escherichia coli Hydrostatic Pressure Heme biology Small-angle X-ray scattering Circular Dichroism Bristol BioDesign Institute General Chemistry Bacterioferritin Cytochrome b Group 0104 chemical sciences Heme B chemistry Ferritins ddc:540 Biophysics biology.protein Thermodynamics Dimerization |
| Zdroj: | Le Vay, K, Carter, B M, Watkins, D W, Tang, T-Y D, Ting, V P, Cölfen, H, Rambo, R P, Smith, A J, Anderson, J L R & Perriman, A W 2020, ' Controlling protein nanocage assembly with hydrostatic pressure ', Journal of the American Chemical Society . https://doi.org/10.1021/jacs.0c07285 |
| DOI: | 10.1021/jacs.0c07285 |
| Popis: | Controlling the assembly and disassembly of nanoscale protein cages for the capture and internalisation of protein or non-proteinaceous components is fundamentally important to a diverse range of bionanotechnological applications. Here, we study the reversible, pressure-induced dissociation of a natural protein nanocage,E. colibacterioferritin (Bfr), using synchrotron radiation small angle X-ray scattering (SAXS) and circular dichroism (CD). We demonstrate that hydrostatic pressures of 450 MPa are sufficient to completely dissociate the Bfr icositetramer into protein dimers, and the reversibility and kinetics of the reassembly process can be controlled by selecting appropriate buffer conditions. We also demonstrate that the heme B prosthetic group present at the subunit dimer interface influences the stability and pressure lability of the cage, despite its location being discrete from the inter-dimer interface that is key to cage assembly. This indicates a major cage-stabilising role for heme within this family of ferritins. |
| Databáze: | OpenAIRE |
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