Abstract
Artificial construction of spherical protein assemblies has attracted considerable attention due to its potential use in nanocontainers, nanocarriers, and nanoreactors. In this work, we demonstrate a novel strategy to construct peptide nanocapsules (artificial viral capsids) decorated with enzymes via interactions between His-tag and Ni-NTA. A β-annulus peptide derived from the tomato bushy stunt virus was modified with Ni-NTA at the C-terminus, which is directed toward the exterior surface of the artificial viral capsid. The β-annulus peptide bearing Ni-NTA at the C-terminus self-assembled into capsids of about 50 nm in diameter. The Ni-NTA-displayed capsids were complexed with recombinant horseradish peroxidase (HRP) with a C-terminal His-tag which was expressed in Escherichia coli. The β-annulus peptide-HRP complex formed spherical assemblies whose sizes were 30–90 nm, with the ζ-potential revealing that the HRP was decorated on the outer surface of the capsid.
Highlights
Natural supramolecular protein nanocapsules such as viral capsids [1,2], clathrin [3], carboxysomes [4], encapsulins [5,6], lumazine synthases [7], and ferritins [8,9] play pivotal roles in many biological processes associated with compartments, transports, and reactions
To construct an artificial viral capsid modified with Ni-NTA at the surface, we designed a Cys-containing β-annulus peptide at the C-terminal side (β-annulus-GGGCG peptide) which was directed toward the exterior of the capsid [34,39,42]
The diameter is comparable to the diameter of unmodified [33] and modified artificial viral capsids [35,38,39,40,41,42,43] self-assembled from β-annulus peptide derivatives, which indicates that Ni-NTA modification of the β-annulus peptide at the C-terminus minimally affected the self-assembling behavior
Summary
Natural supramolecular protein nanocapsules such as viral capsids [1,2], clathrin [3], carboxysomes [4], encapsulins [5,6], lumazine synthases [7], and ferritins [8,9] play pivotal roles in many biological processes associated with compartments, transports, and reactions. One of the main strategies in constructing artificial protein/peptide nanocapusles is by self-assembly of amphiphilic molecules. Nolte et al demonstrated that protein nanocapsules can be self-assembled from “giant amphiphiles” consisting of horseradish peroxidase (HRP) and polystyrene, which are used in peroxidase-based enzymatic cascade reaction systems [23,24,25]. Hayashi et al developed an artificial light-harvesting protein nanocapsule self-assembled from hexameric hemoproteins modified with poly(N-isopropylacrylamide) [26]. Another strategy to construct artificial nanocapsules is to utilize the interactions among secondary structures in the self-assembling protein/peptide subunits [27,28,29,30,31,32]
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