ArticleJournal of the American Chemical Society2020
Amino Acid Residues Determine the Response of Flexible Metal-Organic Frameworks to Guests.
Article in Journal of the American Chemical Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Free-standing ultrathin two-dimensional peptide crystals.Nature chemistry · 2026Article
- Heterometallic 3-D Zn/Ca Metal-Organic Frameworks Based on V-Shaped Angular Tetracarboxylic Ligands as Selective Fluorescence Sensors for Nitroaromatic Explosive Vapors.Inorganic chemistry · 2025Article
- Precise recognition of benzonitrile derivatives with supramolecular macrocycle of phosphorylated cavitand by co-crystallization method.Nature communications · 2024Article
- Soft corrugated channel with synergistic exclusive discrimination gating for CONature communications · 2023Article
- Crystal Engineering of a Chiral Crystalline Sponge That Enables Absolute Structure Determination and Enantiomeric Separation.Crystal growth & design · 2023Article
- Assembly of π-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework.Journal of the American Chemical Society · 2022Article
- Guest Molecule-Mediated Energy Harvesting in a Conformationally Sensitive Peptide-Metal Organic Framework.Journal of the American Chemical Society · 2022Article
- Highly Efficient Removal of Neonicotinoid Insecticides by Thioether-Based (Multivariate) Metal-Organic Frameworks.ACS applied materials & interfaces · 2021Article
- Towards a selective synthetic route for cobalt amino acid complexes and their application in ring opening polymerization ofRSC advances · 2021Article
Corrections and comments
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Authors and funding
13 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flexible metal-organic frameworks (MOFs) undergo structural transformations in response to physical and chemical stimuli. This is hard to control because of feedback between guest uptake and host structure change. We report a family of flexible MOFs based on derivatized amino acid linkers. Their porosity consists of a one-dimensional channel connected to three peripheral pockets. This network structure amplifies small local changes in linker conformation, which are strongly coupled to the guest packing in and the shape of the peripheral pockets, to afford large changes in the global pore geometry that can, for example, segment the pore into four isolated components. The synergy among pore volume, guest packing, and linker conformation that characterizes this family of structures can be determined by the amino acid side chain, because it is repositioned by linker torsion. The resulting control optimizes noncovalent interactions to differentiate the uptake and structure response of host-guest pairs with similar chemistries.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.