Covalent Organic Framework Cladding on Peptide-Amphiphile-Based Biomimetic Catalysts

Area of Science:

• Catalysis
• Materials Science
• Biochemistry

Background:

• Peptide-based biomimetic catalysts offer efficient catalytic activity but suffer from poor operational stability, especially in non-aqueous media.
• Existing catalysts often lack the robustness required for practical applications in diverse chemical transformations.

Purpose of the Study:

• To develop a novel cladding technique for stabilizing peptide biomimetic catalysts within porous covalent organic framework (COF) scaffolds.
• To enhance the catalytic activity and operational stability of peptide catalysts for C-C bond cleavage reactions.

Main Methods:

• Synthesis of peptide-amphiphiles (C10FFVK and C10FFVR) forming nanotubular structures.
• Stabilization of peptide nanotubes within COF backbones (TpAzo and TpDPP) using interfacial crystallization (IC).
• Characterization of the resulting COF-encased peptide nanotubular catalysts.

Main Results:

• Successfully created stable, heterogeneous catalysts (TpAzo-C10FFVK and TpDPP-C10FFVK) with homogeneously distributed peptide nanotubes.
• The TpAzo-C10FFVK catalyst efficiently catalyzed C-C bond cleavage in buffer and organic solvents, demonstrating enzyme-like activity.
• The heterogeneous catalyst was easily recoverable and reusable for multiple cycles, with thin films enabling flow catalysis.

Conclusions:

• The COF cladding technique effectively enhances the stability and recyclability of peptide biomimetic catalysts.
• Lysine residues in the peptide sequence are crucial for the observed catalytic activity in C-C bond cleavage.
• This approach provides a promising strategy for developing robust and versatile catalysts for chemical synthesis.