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The exploration of chiral crystalline porous materials, such as metal-organic complexes (MOCs) or metal-organic frameworks (MOFs), has been one of the most exciting recent developments in materials science owing to their widespread applications in enantiospecific processes. However, achieving specific tight-affinity binding and remarkable enantioselectivity toward important biomolecules is still challenging. Perhaps most critically, the lack of adaptability, compatibility, and processability in these materials severely impedes practical applications in chemical engineering and biological technology. In this Perspective, artificial metal-peptide assemblies (MPAs), which are achieved by the assembly of peptides and metals with nanometer-sized cavities or pores, is a new development that could address the current bottlenecks of chiral porous materials. Bioinspired assembly of pore-forming MPAs is not foreign to biological systems and has granted scientists an unprecedented level of control over the chiral recognition sites, conformational flexibility, cavity sizes, and hydrophilic segments through ultrafine-tuning of peptide-derived linkers. We will specifically discuss exemplary MPAs including structurally well-defined metal-peptide complexes and highly crystalline metal-peptide frameworks. With insights from these structures, the peptide assembly and folding by the closer cooperation of metal coordination and noncovalent interactions can create adaptable protein-like nanocavities undergoing a myriad of conformational variations that is reminiscent of enzymatic pockets. We also consider challenges to advancing the field, where the deployment of side-chain groups and manipulation of amino acid sequences are more likely to access the programmable, genetically encodable peptide-mediated porous materials, thus contributing to the enhanced enantioselective recognition as well as enabling key biochemical processes in next-generation versatile biomimetic materials.
Dong et al. (Thu,) studied this question.