Back Cover: High‐Throughput Screening (HTS) by NMR Guided Identification of Novel Agents Targeting the Protein Docking Domain of YopH (ChemMedChem 8/2016). (20th April 2016)

• Record Type: Journal Article
• Authors: Bottini, Angel; Wu, Bainan; Barile, Elisa; De, Surya K.; Leone, Marilisa; Pellecchia, Maurizio
• Is Part Of: ChemMedChem. Volume 11:Number 8(2016)
• Page Start: 947
• Page End: 947
• Publication Date: 2016-04-20
• Subjects: combinatorial libraries -- high-throughput screening (HTS) -- NMR spectroscopy -- peptides -- protein–protein interactions -- YopH; Pharmaceutical chemistry -- Periodicals; 615.19005
• DOI: 10.1002/cmdc.201600186
• Languages: English
• ISSNs: 1860-7179

Abstract

Abstract : The back cover picture shows the high‐throughput screening (HTS) by NMR approach. Guided by NMR spectroscopy [background picture showing portions of 15 N, 1 H correlation spectra of the target, in the absence (cyan) and presence (yellow) of a binding ligand], initial weak binders can be identified among mixtures of >100 000 peptide mimetics, arranged in positional scanning mode (top left). Subsequent rapid optimization steps can lead to potent peptide mimetics with nanomolar affinity, as measured by isothermal titration calorimetry (ITC, top right). After identification of the initial tri‐peptidoid (bottom left), the approach entailed the synthesis and testing of only about a dozen molecules to obtain the potent binder (bottom right). More information can be found in the Full Paper by Maurizio Pellecchia et al. onpage 919 in Issue 8, 2016 (DOI:10.1002/cmdc.201500441 ).