Cover image for Vol. 17 Issue 16

Editor: Meghan Campbell; Editorial Board Chairs: Thomas Carell, Donald Hilvert, Barbara Imperiali

Online ISSN: 1439-7633

Associated Title(s): ChemCatChem, ChemMedChem, ChemPhysChem, ChemSusChem

8_09/2007Cover Picture: Embedding the Amyloid β-Peptide Sequence in Green Fluorescent Protein Inhibits Aβ Oligomerization (ChemBioChem 9/2007)

The cover picture shows a green fluorescent protein (GFP) variant in which an amyloid β-peptide (Aβ) sequence is embedded. Through self recognition Aβ can aggregate to toxic species such as soluble oligomers that form β-sheet structures, and this oligomerization is closely related to Alzheimer's disease (AD). Embedding the Aβ sequence in a GFP scaffold that contains stable β-sheet structures generates a pseudo-Aβ surface on GFP. Thus, the GFP variant can bind to Aβ with high affinity, and their interaction effectively inhibits Aβ oligomerization. This strategy could be applied to other amyloid-related diseases such as prion and Parkinson's diseases. For more information see the full paper by T. Takahashi et al. on p. 985 ff.

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