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    PDZ domains play crucial roles in cell signaling processes and are therefore attractive targets for the development of therapeutic inhibitors. In many cases, C-terminal peptides are the physiological binding partners of PDZ domains. To identify both native ligands and potential inhibitors we have screened arrays synthesized by the process of inverted peptides (PIPE), a variant of SPOT synthesis that generates peptides with free C-termini. Here, we present the development of a new functionalized cellulose membrane as solid support along with the optimized PIPEPLUS technology. Improved resolution and accuracy of the synthesis were shown with peptide arrays containing both natural and non-natural amino acids. These new screening possibilities will advance the development of active, selective and metabolically stable PDZ interactors. Copyright © 2017 Elsevier Ltd. All rights reserved.

    Citation

    Quentin Seisel, Marisa Rädisch, Nicholas P Gill, Dean R Madden, Prisca Boisguerin. Optimization of the process of inverted peptides (PIPEPLUS) to screen PDZ domain ligands. Bioorganic & medicinal chemistry letters. 2017 Jul 15;27(14):3111-3116

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    PMID: 28549735

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