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Disrupting Protein–Protein Interfaces Using GRID Molecular Interaction Fields

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Disruption of Protein-Protein Interfaces

Abstract

Protein–protein interactions (PPI) are central to most biological process and include aspects such as viral self-assembly, cell proliferation, growth, differentiation, signal transduction, and programmed cell death [1], and the last decade has seen an explosion of interest [2–4]. The human interactome has been estimated to involve ~25,000 proteins and ~650,000 interactions [5], and currently, only about 0.3 % of these have been identified [6]. In silico approaches targeting PPIs are still limited, however the versatility of GRID Molecular Interaction Fields is demonstrated through several case studies that explore how novel PPI inhibitors can be identified.

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Acknowledgments

The authors would like to thank Jon Mason and Thierry Langer for their involvement in the original FLAP and GBPM methodology.

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Authors and Affiliations

  1. Molecular Discovery Limited, 215 Marsh Road, Pinner, Middlesex, London, HA5 5NE, UK

    Simon Cross

  2. Laboratory for Chemometrics and Cheminformatics, Chemistry Department, University of Perugia, Via Elce di sotto 10, I-06123, Perugia, Italy

    Massimo Baroni & Gabriele Cruciani

  3. Laboratory of Computational Medicinal Chemistry, Department of “Scienze della Salute”, University “Magna Græcia” of Catanzaro, Viale Europa, Loc, Germaneto, 88100, Catanzaro, Italy

    Francesco Ortuso & Stefano Alcaro

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  1. Simon Cross
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  2. Massimo Baroni
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  3. Francesco Ortuso
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  4. Stefano Alcaro
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  5. Gabriele Cruciani
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Correspondence to Simon Cross .

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  1. , Department of Biotechnology, Chemistry a, University of Siena, Siena, Siena, I-53100, Italy

    Stefano Mangani

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Cross, S., Baroni, M., Ortuso, F., Alcaro, S., Cruciani, G. (2013). Disrupting Protein–Protein Interfaces Using GRID Molecular Interaction Fields. In: Mangani, S. (eds) Disruption of Protein-Protein Interfaces. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-37999-4_3

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