Cover Picture: Enantioselective Photochromism of Diarylethenes in Human Serum Albumin (Chem. Eur. J. 29/2013). Issue 29 (8th July 2013)

• Record Type: Journal Article
• Authors: Fukagawa, Mai; Kawamura, Izuru; Ubukata, Takashi; Yokoyama, Yasushi
• Is Part Of: Chemistry. Volume 19:Issue 29(2013)
• Page Start: 9401
• Page End: 9401
• Publication Date: 2013-07-08
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201390105
• Languages: English
• ISSNs: 0947-6539

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Controlled construction</bold> of molecular chirality is central to modern molecular organic chemistry. In their Communication on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">page 9434 ff., </ext-link> Y. Yokoyama et al. demonstrate that human serum albumin (HSA), a nonenzymatic protein in blood, acts as a mold to fix the conformation of thermally irreversible photochromic diarylethenes and transfers chirality in photoreactions. A bisthienylperfluorocyclopentene with a hydroxy group at each end of the molecule, incorporated in the HSA pocket, yields the colored cyclic form in 63 % <italic>ee</italic> at 25 °C and 71 % <italic>ee</italic> at −4 °C. The X‐ray image of HSA was provided courtesy of the RCSB PDB (Code 4K2C with Simple Viewer 4.1.0).<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg26mfgr0c" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>