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Guest‐Adaptable and Water‐Stable Peptide‐Based Porous Materials by Imidazolate Side Chain Control
Author(s) -
Katsoulidis Alexandros P.,
Park Kyo Sung,
Antypov Dmytro,
MartíGastaldo Carlos,
Miller Gary J.,
Warren John E.,
Robertson Craig M.,
Blanc Frédéric,
Darling George R.,
Berry Neil G.,
Purton John A.,
Adams Dave J.,
Rosseinsky Matthew J.
Publication year - 2014
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201307074
Subject(s) - imidazolate , zeolitic imidazolate framework , imidazole , chemistry , histidine , crystallography , side chain , dipeptide , peptide , residue (chemistry) , deprotonation , stereochemistry , chemical engineering , organic chemistry , metal organic framework , polymer , ion , biochemistry , enzyme , adsorption , engineering
The peptide‐based porous 3D framework, ZnCar, has been synthesized from Zn 2+ 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 m 2 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 H 2 O 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.