Abstract
The synthesis of chiral metal–organic frameworks (MOFs) is highly relevant for asymmetric heterogenous catalysis, yet very challenging. Chiral MOFs with MOF‐74 topology were synthesised by using post‐synthetic modification with proline. Vibrational circular dichroism studies demonstrate that proline is the source of chirality. The solvents used in the synthesis play a key role in tuning the loading of proline and its interaction with the MOF‐74 framework. In N,N′‐dimethylformamide, proline coordinates monodentate to the Zn2+ ions within the MOF‐74 framework, whereas it is only weakly bound to the framework when using methanol as solvent. Introducing chirality within the MOF‐74 framework also leads to the formation of defects, with both the organic linker and metal ions missing from the framework. The formation of defects combined with the coordination of DMF and proline within the framework leads to a pore blocking effect. This is confirmed by adsorption studies and testing of the chiral MOFs in the asymmetric aldol reaction between acetone and para‐nitrobenzaldehyde.
Highlights
Chirality plays a key role in the understanding of biochemistry[1,2] and it remains a long-standing enigma for explaining the origin of life because all chiral amino acids in proteins and enzymes exist only in their l form.[3]
The first approach to synthesise a chiral Zn-metal–organic frameworks (MOFs)-74 topology aimed at using d- and l-Pro as chiral inductor during the typical synthesis of Zn-MOF-74.[47]. This molecule has the ability to interact with the MOF framework via hydrogen bonding with the carboxylate groups of the organic linkers or through coordination to the open sites on the Zn2+ ions.[48]
We hypothesised that the interaction of l- or d-Pro with Zn-MOF74 may lead to a chiral framework and that proline, as auxiliary ligand, will lead to a long-range chirality order
Summary
Chirality plays a key role in the understanding of biochemistry[1,2] and it remains a long-standing enigma for explaining the origin of life because all chiral amino acids in proteins and enzymes exist only in their l form.[3]. Strudwick Current address: Paul Scherrer Institute, ETH Zürich Forschungsstrasse 111, 5232 Villigen PSI, Zürich (Switzerland)
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