Cover Picture: Peptides Targeting EGF Block the EGF–EGFR Interaction (ChemBioChem 8/2016). (5th April 2016)

• Record Type: Journal Article
• Authors: Guardiola, Salvador; Díaz‐Lobo, Mireia; Seco, Jesús; García, Jesús; Nevola, Laura; Giralt, Ernest
• Is Part Of: Chembiochem. Volume 17:Number 8(2016)
• Page Start: 642
• Page End: 642
• Publication Date: 2016-04-05
• Subjects: cancer therapy -- membrane receptors -- peptides -- protein–protein interaction -- SAW; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201600144
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract : The cover picture shows the dimerization process that EGFR undergoes upon its activation by the binding of EGF (shown as a green surface) to the extracellular domain. The central involvement of the EGF–EGFR pathway in tumour cell proliferation makes it a key target for cancer therapy. The article describes a novel approach to block EGFR activation by disrupting the interaction between EGF and EGFR. Using docking and receptor hotspot mimicry techniques, a variety of peptide inhibitors targeting EGF were designed, and their binding to EGF was characterized by a range of biophysical techniques. A segment in domain I of EGFR (shown in red) that is relevant for EGF recognition was the cornerstone for developing a cyclic peptide (cp28) that proved to successfully block the EGF–EGFR interaction. More information can be found in the full paper by L. Nevola, E. Giralt et al. onpage 702 in Issue 8, 2016 (DOI:10.1002/cbic.201500525 ).