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Bottom-up construction of chiral metal-peptide assemblies from metal cluster motifs
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Bottom-up construction of chiral metal-peptide assemblies from metal cluster motifs
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Bottom-up construction of chiral metal-peptide assemblies from metal cluster motifs
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Journal Article
Bottom-up construction of chiral metal-peptide assemblies from metal cluster motifs
2024
Overview
The exploration of artificial metal-peptide assemblies (MPAs) is one of the most exciting fields because of their great potential for simulating the dynamics and functionality of natural proteins. However, unfavorable enthalpy changes make forming discrete complexes with large and adaptable cavities from flexible peptide ligands challenging. Here, we present a strategy integrating metal-cluster building blocks and peptides to create chiral metal-peptide assemblies and get a family of enantiopure [
R-/S-
Ni
3
L
2
]
n
(n = 2, 3, 6) MPAs, including the
R-/S-
Ni
6
L
4
capsule, the
S-
Ni
9
L
6
trigonal prism, and the
R-/S-
Ni
18
L
12
octahedron cage. X-ray crystallography shows MPA formation reactions are highly solvent-condition-dependent, resulting in significant changes in ligand conformation and discrete cavity sizes. Moreover, we demonstrate that a structure transformation from Ni
18
L
12
to Ni
9
L
6
in the presence of benzopyrone molecules depends on the peptide conformational selection in crystallization. This work reveals that a metal-cluster building block approach enables facile bottom-up construction of artificial metal-peptide assemblies.
The use of metal clusters to construct artificial protein-mimic structures with adaptable cavities has potential for simulating the dynamics and functionality of natural proteins. Here, the authors develop a family of chiral metal-peptide assemblies using {Ni3} clusters and flexible peptides, resulting in structures such as octahedral cages, trigonal prisms, and capsules.
