Guest-adaptable and water-stable peptide-based porous materials by imidazolate side chain control.
Guest-adaptable and water-stable peptide-based porous materials by imidazolate side chain control.
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DOI:
10.1002/anie.201307074
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发表时间:
2014-01-03
影响因子:
16.6
通讯作者:
Rosseinsky, Matthew J.
中科院分区:
文献类型:
--
作者:
Katsoulidis, Alexandros P.;Park, Kyo Sung;Antypov, Dmytro;Marti-Gastaldo, Carlos;Miller, Gary J.;Warren, John E.;Robertson, Craig M.;Blanc, Frederic;Darling, George R.;Berry, Neil G.;Purton, John A.;Adams, Dave J.;Rosseinsky, Matthew J.
The peptide-based porous 3D framework, ZnCar, has been synthesized from Zn2+ and the natural dipeptide carnosine (β-alanyl-L-histidine). Unlike previous extended peptide networks, the imidazole side chain of the histidine residue is deprotonated to afford Zn–imidazolate chains, with bonding similar to the zeolitic imidazolate framework (ZIF) family of porous materials. ZnCar exhibits permanent microporosity with a surface area of 448 m2 g−1, and its pores are 1D channels with 5 Å openings and a characteristic chiral shape. This compound is chemically stable in organic solvents and water. Single-crystal X-ray diffraction (XRD) showed that the ZnCar framework adapts to MeOH and H2O guests because of the torsional flexibility of the main His-β-Ala chain, while retaining the rigidity conferred by the Zn–imidazolate chains. The conformation adopted by carnosine is driven by the H bonds formed both to other dipeptides and to the guests, permitting the observed structural transformations.
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