Published in
Wiley, Angewandte Chemie International Edition, 1(53), p. 193-198, 2013
Wiley, Angewandte Chemie, 1(126), p. 197-202, 2013
Links
- ORCID
- ORCID
- Wiley
- Wiley
- [www.ncbi.nlm.nih.gov] | PDF
- [repository.liv.ac.uk]
- [purl.org]
- [eprints.gla.ac.uk]
- [www.researchgate.net] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [www.ncbi.nlm.nih.gov] | PDF
- [europepmc.org] | PDF
- [eprints.gla.ac.uk] | PDF
Tools
Guest-Adaptable and Water-Stable Peptide-Based Porous Materials by Imidazolate Side Chain Control**
,
Dmytro Antypov,
Park Ks,
Carlos Martí-Gastaldo,
Gary J. Miller,
Miller Gj,
John E. Warren,
Warren Je,
Craig M. Robertson,
Robertson Cm,
Frédéric Blanc,
George R. Darling,
Darling Gr
and other authors.
Full text: Download
Abstract
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 H2 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.