Peptide metal-organic frameworks under pressure: flexible linkers for cooperative compression

Dalton Transactions : an International Journal of Inorganic Chemistry
José Navarro-SánchezC Martí-Gastaldo

Abstract

We investigate the structural response of a dense peptide metal-organic framework using in situ powder and single-crystal X-ray diffraction under high-pressures. Crystals of Zn(GlyTyr)2 show a reversible compression by 13% in volume at 4 GPa that is facilitated by the ability of the peptidic linker to act as a flexible string for a cooperative response of the structure to strain. This structural transformation is controlled by changes to the conformation of the peptide, which enables a bond rearrangement in the coordination sphere of the metal and changes to the strength and directionality of the supramolecular interactions specific to the side chain groups in the dipeptide sequence. Compared to other structural transformations in Zn(ii) peptide MOFs, this behaviour is not affected by host/guest interactions and relies exclusively on the conformational flexibility of the peptide and its side chain chemistry.

References

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Citations

May 29, 2019·Dalton Transactions : an International Journal of Inorganic Chemistry·Mirosław MączkaWaldeci Paraguassu
Mar 21, 2019·Physical Chemistry Chemical Physics : PCCP·Meysam AkhtarJacek B Jasinski
Mar 14, 2019·Inorganic Chemistry·Enrico BandielloCatalin Popescu
Aug 21, 2019·Journal of the American Chemical Society·M Nieves Corella-OchoaJosé Ramón Galán-Mascarós

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Methods Mentioned

BETA
X-ray
Scanning
circular dichroism

Software Mentioned

EosFit7
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