Porous Peptide Frameworks with Tertiary Structures
Year: 2026
Type: preprint
Abstract: Complex functions such as selective molecular recognition and catalysis arise from the precise three-dimensional arrangement of functional groups that are best exemplified in the protein tertiary structure. Reproducing this level of structural precision and chemical modularity in abiotic materials remains a fundamental challenge. Here, we show that peptide self-assembly into porous crystalline frameworks can result in tuneable tertiary structures composed of helix, loop, and β-strand motifs within a single chain that is only 15–19 amino acids in length, which is less than 6% the size of the average protein. These peptide frameworks were designed by hybridising a framework-forming 11-residue α-helix with variable sequence fragments, yielding extended lattices with channels lined by 8–10 distinct side chains, as confirmed by single-crystal X-ray diffraction (SC-XRD). As a proof-of-principle, these pores can be programmed to encode various constellations of functional groups capable of selective molecular recognition, including near quantitative discrimination of ATP over ADP and chain-length-dependent recognition of perfluoroalkyl carboxylic acids. These results demonstrate that a well-defined tertiary structure can exist in very short peptides and can impart programmable, protein-like function to synthetic porous materials.
Source: ChemRxiv
Institutions: University of Illinois Chicago, Northwestern University
Subfield: Biomaterials
Field: Materials Science
Domain: Physical Sciences
Open Access status: green
OpenAlex ID: W7165202111
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