Guest‐Adaptable and Water‐Stable Peptide‐Based Porous Materials by Imidazolate Side Chain Control1. (2nd December 2013)

• Record Type: Journal Article
• Authors: Katsoulidis, Alexandros P.; Park, Kyo Sung; Antypov, Dmytro; Martí‐Gastaldo, 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.
• Is Part Of: Angewandte Chemie. Volume 126:Number 1(2014)
• Page Start: 197
• Page End: 202
• Publication Date: 2013-12-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201307074
• Languages: English
• ISSNs: 0044-8249

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>The peptide‐based porous 3D framework, ZnCar, has been synthesized from Zn²⁺ and the natural dipeptide carnosine (β‐alanyl‐<sc>L</sc>‐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.</p> </abstract>