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Foods
2023 Oct 25;1221:. doi: 10.3390/foods12213903.
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Preparation and Unique Three-Dimensional Self-Assembly Property of Starfish Ferritin.
Zhang C
,
Chen X
,
Liu B
,
Zang J
,
Zhang T
,
Zhao G
.
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The structure and assembly properties of ferritin derived from aquatic products remain to be explored. Constructing diverse three-dimensional (3D) protein architectures with the same building blocks has important implications for nutrient delivery, medicine and materials science. Herein, ferritin from Asterias forbesii (AfFer) was prepared, and its crystal structure was resolved at 1.91 Å for the first time. Notably, different from the crystal structure of other reported ferritin, AfFer exhibited a BCT lattice arrangement in its crystals. Bioinspired by the crystal structure of AfFer, we described an effective approach for manufacturing 3D porous, crystalline nanoarchitectures by redesigning the shared protein interface involved in different 3D protein arrays. Based on this strategy, two 3D superlattices of body-centered tetragonal and simple cubicwere constructed with ferritin molecules as the building blocks. This study provided a potentially generalizable strategy for constructing different 3D protein-based crystalline biomaterials with the same building blocks.
Scheme 1. Schematic representation of the construction and interconversion of BCT and SC ferritin arrays. The Glu10, Asn9, and Lys120 of each ferritin subunit near its C3 interfaces are highlighted in yellow, and the His/Phe mutation around the C4 interfaces of ferritin are highlighted in pink.
Figure 1. X-ray diffraction (PDB ID: 8IQV) characterization of AfFer. (A) Optical microscope image of AfFer crystals at pH 8.0, 15% (v/v) ethanol, and 200 mM MgCl2. (B) Side and top views of the 3D AfFer arrays in the crystal structure. (C) Close-up view of the proline residues at the C4 interface between two adjacent AfFer molecules. (D) Close-up view of the electrostatic interactions between two adjacent AfFer molecules along the C3 interface. (E) The C3 interfaces directly involved in AfFer’s intermolecular interactions. The subunits involved in electrostatic interaction are highlighted as dark pink and dark turquoise, and other subunits constituting the C3 interface are highlighted as pale pink and turquoise.
Figure 2. Characterization of the P156HAfFer assemblies at pH 8.0, 15%(v/v) alcohol, and 200 mM MgCl2. (A–C) TEM images of the P156HAfFer assemblies. (D) Real map of the inverted FFT from (C). The protein concentration was 2.0 µM. (E) 2D SAXS pattern of the P156HAfFer assemblies. (F) Radially averaged 1D SAXS data of the ferritin assemblies. The simulated diffraction pattern is shown in blue.
Figure 3. Body-centered tetragonal crystal structure of P156HAfFer (PDB ID: 8IQY). (A) Optical microscope image of the crystal. (B) Side and top views of the 3D array in the crystal structure. (C) Tetragonal lattice. (D) Close-up view of the electrostatic interactions between two adjacent P156HAfFer molecules along C3 interface. (E) Close-up view of His-mediated π–π interactions between two adjacent P156HAfFer molecules along the C4 interface.
Figure 4. Characterization of the P156HAfFer assemblies at pH 8.0 and 200 µM NiCl2. (A–C) TEM images of the P156HAfFer assemblies. (D) Real map from the inverted FFT of (B). The protein concentration was 2.0 µM. (E) 2D SAXS pattern of the P156HAfFer assemblies. (F) Radially averaged 1D SAXS data of the ferritin assemblies. Simulated diffraction pattern is shown in blue.
Figure 5. Simple cubic crystal structure of P156HAfFer (PDB ID: 8IQX). (A) Optical microscope image of the crystal. (B) The SC array in the crystal structure. (C) Close-up view of the interfacial interactions between two adjacent P156HAfFer molecules, including electrostatic and π–π stacking interactions. (D) Stacking pattern of two adjacent P156HAfFer molecules along the C4 interface.
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