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BIOMIMETIC MATERIALS

Porous and permutable peptide frameworks

Nature Chemistry volume 14, pages 852–854 (2022)Cite this article

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The rational synthesis of advanced porous materials that mimic the behaviours of biological proteins remains challenging. Now, a distinct type of crystalline porous peptide framework has been prepared through bioinspired noncovalent assembly, enabling chemical tuning of the properties and functions of the pore environments.

Over the past three decades, crystalline porous materials, such as metal–organic frameworks (MOFs) and covalent organic frameworks, have emerged as an exciting research frontier of chemistry and materials science1,2. The resulting intrinsic porosity and high surface area are of interest for a range of applications, including gas adsorption and separation, sensing and catalysis. These structures often have a high prevalence of rigid aromatic components and generally form well-crystallized products with few geometric degrees of freedom. But such structures tend to have rigid internal cavities that may be disadvantageous, as recent findings have shown that adaptable (flexible) pore environments have superior guest-to-framework interactions3. Furthermore, materials with high concentration of rigid aromatic motifs also show substantial hydrophobicity, which greatly affects the surface compatibility for materials chemistry and biocompatibility for biologic systems, severely impeding practical applications.

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Fig. 1: Self-assembly, crystal structures and host−guest chemistry of porous peptide frameworks.

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  1. Twitter: @ZhaoGroupNUS

Authors and Affiliations

  1. Department of Chemical & Biomolecular Engineering, National University of Singapore, Queenstown, Singapore

    Jinqiao Dong & Dan Zhao

  2. School of Chemistry and Chemical Engineering, State Key Laboratory of Metal Matrix Composites, Shanghai Jiao Tong University, Shanghai, China

    Jinqiao Dong

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  1. Jinqiao Dong
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  2. Dan Zhao
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Correspondence to Jinqiao Dong or Dan Zhao.

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Dong, J., Zhao, D. Porous and permutable peptide frameworks. Nat. Chem. 14, 852–854 (2022). https://doi.org/10.1038/s41557-022-01011-1

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  • DOI: https://doi.org/10.1038/s41557-022-01011-1

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