Artificial Protein Cage with Unusual Geometry and Regularly Embedded Gold Nanoparticles

Majsterkiewicz, Karolina; Biela, Artur; Maity, Sourav; Sharma, Mohit; Piette, Bernard; Kowalczyk, Agnieszka; Gaweł, Szymon; Chakraborti, Soumyananda; Roos, Wouter H.; Heddle, Jonathan G.

doi:10.1021/acs.nanolett.1c04222

Cited by 17 publications

(14 citation statements)

References 38 publications

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“…This is motivated by the fact that p-cages with such a deformation are noticeably irregular to the naked eye, but not excessively so. It is also motivated by the fact that nano-cages with deformation close to or exceeding 2% are known to be likely (AP Biela 2019, personal communication) [ 11 ].…”

Section: Introductionmentioning

confidence: 99%

Characterization of near-miss connectivity-invariant homogeneous convex polyhedral cages

2022

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Following the discovery of a nearly symmetric protein cage, we introduce the new mathematical concept of a near-miss polyhedral cage (p-cage) as an assembly of nearly regular polygons with holes between them. We then introduce the concept of the connectivity-invariant p-cage and show that they are related to the symmetry of uniform polyhedra. We use this relation, combined with a numerical optimization method, to characterize some classes of near-miss connectivity-invariant p-cages with a deformation below 10% and faces with up to 17 edges.

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Section: Introductionmentioning

confidence: 99%

Characterization of near-miss connectivity-invariant homogeneous convex polyhedral cages

2022

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“…As a powerful tool to visualize the structural detail of protein assemblies, we used cryo-EM measurements to determine the structural details of the Naph @(MIX|3:3) complex. ,, The three-dimensional structure of Naph @(MIX|3:3) was successfully determined at 2.81 Å resolution (Figure a; see Figure S8 for the detail of data collection and processing). Within the Naph @(MIX|3:3) mixture, Naph @TkPrx*F42C and Naph @TkPrx*F76C were placed in an alternating arrangement, confirmed by the positions of the cysteine residues of the two mutants modified by Naph moiety.…”

Section: Resultsmentioning

confidence: 99%

Unnaturally Distorted Hexagonal Protein Ring Alternatingly Reorganized from Two Distinct Chemically Modified Proteins

et al. 2023

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In this study, we constructed a semiartificial protein assembly of alternating ring type, which was modified from the natural assembly state via incorporation of a synthetic component at the protein interface. For the redesign of a natural protein assembly, a scrap-and-build approach employing chemical modification was used. Two different protein dimer units were designed based on peroxiredoxin from Thermococcus kodakaraensis, which originally forms a dodecameric hexagonal ring with six homodimers. The two dimeric mutants were reorganized into a ring by reconstructing the protein–protein interactions via synthetic naphthalene moieties introduced by chemical modification. Cryo-electron microscopy revealed the formation of a uniquely shaped dodecameric hexagonal protein ring with broken symmetry, distorted from the regular hexagon of the wild-type protein. The artificially installed naphthalene moieties were arranged at the interfaces of dimer units, forming two distinct protein–protein interactions, one of which is highly unnatural. This study deciphered the potential of the chemical modification technique that constructs semiartificial protein structures and assembly hardly accessible by conventional amino acid mutations.

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“…Significant differences in angles around four-fold holes and bowtie holes suggest that large flexibility of the constituent proteins allows necessary deformation. These deformations result in a decrease in the overall symmetry of the particle to C2 in comparison with TRAP K35C‑Au large and small cages (octahedral and tetrahedral, respectively). The angles formed also depend on the type of the ring.…”

Section: Resultsmentioning

confidence: 99%

Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change

et al. 2022

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Artificial protein cages are constructed from multiple protein subunits. The interaction between the subunits, notably the angle formed between them, controls the geometry of the resulting cage. Here, using the artificial protein cage, “TRAP-cage”, we show that a simple alteration in the position of a single amino acid responsible for Au(I)-mediated subunit–subunit interactions in the constituent ring-shaped building blocks results in a more acute dihedral angle between them. In turn, this causes a dramatic shift in the structure from a 24-ring cage with an octahedral symmetry to a 20-ring cage with a C2 symmetry. This symmetry change is accompanied by a decrease in the number of Au(I)-mediated bonds between cysteines and a concomitant change in biophysical properties of the cage.

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Artificial Protein Cage with Unusual Geometry and Regularly Embedded Gold Nanoparticles

Cited by 17 publications

References 38 publications

Characterization of near-miss connectivity-invariant homogeneous convex polyhedral cages

Characterization of near-miss connectivity-invariant homogeneous convex polyhedral cages

Unnaturally Distorted Hexagonal Protein Ring Alternatingly Reorganized from Two Distinct Chemically Modified Proteins

Shape-Morphing of an Artificial Protein Cage with Unusual Geometry Induced by a Single Amino Acid Change

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