Disulfide-mediated reversible two-dimensional self-assembly of protein nanocages

Abstract

Disulfide-mediated 2D protein self-assembly was achieved by single point mutation of hot spots at the C4 interface of ferritin.

Characteristics of silver carp surimi gel under high temperature (≥100 °C): quality changes, water distribution and protein pattern

“…This might be due to heat treatment, which aggravated the movement of the molecules and at the same time changed the structure of the protein molecules, resulting in an increase in electrostatic interactions (Wang et al ., 2020). Changes in disulphide bonds were inconsistent with previous research reporting that high temperature might cause uncontrolled rapid oxidation of free sulphydryl groups to form disulphide bonds (Zhou et al, 2019). This might be due to the oxidation of sulphydryl and disulphide bonds in the protein to form guanine or cleavage to generate H 2 S under high temperature conditions.…”

Converting histidine-induced 3D protein arrays in crystals into their 3D analogues in solution by metal coordination cross-linking

“…While a variety of different dimensional protein assemblies have been reported by using different noncovalent and covalent interactions as driving forces 11,[21][22][23][24][25][26][27][28][29][30][31][32] , the majority of the designed PPIs for high ordered protein assemblies is based on single noncovalent or covalent interaction as a driving force. Here, we demonstrate that a combination of π-π interaction and metal coordination represents an effective way to build 3D protein arrays in crystals and solution.…”

“…Such naturally occurring protein assemblies have been extensively studied by synthetic biologists and chemists in the field of nanoscience for exploring biomimetic methods to prepare new nanoscale protein materials with valuable functions [13][14][15][16][17][18][19][20] . Importantly, some considerable applications of designing protein and constructing multifarious supramolecular protein material by varied strategies 11,[21][22][23][24][25][26][27][28][29][30][31][32] for scientists had been carried out to rival the size and functionality of natural protein. These engineered protein assemblies are competitive owing to their excellent potential biocompatibility and biofunctionality.…”

Protein Assembly by Design

“… Alternatively, building blocks that possess 2D or 3D symmetry, such as the C 4 symmetric L -rhamnulose-1-phosphate aldolase (RhuA) and the octahedral ferritin, can be engineered in their vertices with Cys residues to self-assemble into disulfide-mediated 2D lattices (see section ). − Particularly, the 2D C98 RhuA lattices, described in more detail in section , illustrate the key importance of the reversibility of disulfide bonds in the formation of defect-free lattices, while also highlighting how the flexibility of these bonds can give rise to coherent lattice dynamics (section ). − Other types of covalent linkages have also been used to drive protein self-assembly, such as native chemical ligation, Tyr dimerization, and sulfo-NHS/EDC coupling; however, the irreversibility of these linkages generally translates into a lack of order and structural homogeneity.…”

“…It has arguably proven to be the most versatile building block available in the design and construction of protein assemblies, as demonstrated by the broad range of ferritin-based ordered 2D and 3D lattices reported just in the past decade. The Zhao Group employed several types of modifications at the C 4 axis of the ferritin cage to enable the formation of square 2D lattices. ,,, Zhou et al applied a disulfide bonding strategy to make covalently linked 2D lattices from homo-oligomeric human heavy chain ferritin (HuHF) by installing Cys residues near the C 4 axes of the cage (C162) . This single mutation positioned four Cys residues in close proximity to each other and created a “hot spot” for interactions, to construct a superlattice upon slow oxidation in the presence of βME (Figure ).…”