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Front Cover: Structural Basis of the Light‐Switchable Interaction between an Azobenzene Side Chain in a Biosynthetic Protein and α‐Cyclodextrin (ChemistryOpen 1/2026)
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Front Cover: Structural Basis of the Light‐Switchable Interaction between an Azobenzene Side Chain in a Biosynthetic Protein and α‐Cyclodextrin (ChemistryOpen 1/2026)
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Front Cover: Structural Basis of the Light‐Switchable Interaction between an Azobenzene Side Chain in a Biosynthetic Protein and α‐Cyclodextrin (ChemistryOpen 1/2026)
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Journal Article
Front Cover: Structural Basis of the Light‐Switchable Interaction between an Azobenzene Side Chain in a Biosynthetic Protein and α‐Cyclodextrin (ChemistryOpen 1/2026)
2026
Overview
The Front Cover illustrates the specific host/guest complex formation between the light‐switchable noncanonical amino acid /p/‐(phenylazo)‐L‐phenylalanine (Pap) in its low‐energy /trans/‐state and α‐cyclodextrin (α‐CD), which is elucidated by X‐ray crystallographic analysis of super‐folder green fluorescent protein (sfGFP) as carrier for the Pap side chain. Upon illumination with mild UV‐A light, Pap switches to the /cis/‐configuration and the complex dissociates, which can be utilized for the affinity purification of sfGFP(39Pap) on an α‐CD affinity column. More information can be found in the Research Article by Arne Skerra and co‐workers (DOI: 10.1002/open.202500471).
Publisher
Wiley
Subject
