{"product_id":"protein-surface-recognition-9780470059050","title":"Protein Surface Recognition","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eA new perspective on the design of molecular therapeutics is emerging. This new strategy emphasizes the rational complementation of functionality along extended patches of a protein surface with the aim of inhibiting protein\/protein interactions.\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTrade Review\u003c\/b\u003e\u003cbr\u003e\"This book picks up this trend and provides an excellent overview of the current topics in the field of PPI modulation by small molecules and peptides. . . Taken together, this excellent book is very suitable both as an introduction to the field, as well as a compendium for readers already familiar with the chemical approach of modulating PPIs.\" (ChemMedChem, 2011)  \u003cp\u003e \u003c\/p\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003ePreface.  \u003cp\u003eList of Contributors.\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART I PRINCIPLES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1\u003c\/b\u003e \u003cb\u003eThe Discovery and Characterization of Protein-Protein Interactions\u003c\/b\u003e (\u003ci\u003eC.W. Bertoncini, A. Higueruelo, and X. Salvatella\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e1.1 Introduction.\u003c\/p\u003e \u003cp\u003e1.2 Techniques to Identify Protein-Protein Interactions.\u003c\/p\u003e \u003cp\u003e1.3 Techniques to Characterize Protein-Protein Interactions.\u003c\/p\u003e \u003cp\u003e1.4 Structure and Dynamics of Protein Complexes.\u003c\/p\u003e \u003cp\u003e1.5 Protein-Protein Complexes as Therapeutic Targets.\u003c\/p\u003e \u003cp\u003e1.6 Conclusions.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Biophysics of Protein-Protein Interactions\u003c\/b\u003e (\u003ci\u003eIrene Luque\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e2.1 Introduction.\u003c\/p\u003e \u003cp\u003e2.2 Intermolecular Forces in Protein Recognition.\u003c\/p\u003e \u003cp\u003e2.3 Basic Binding Thermodynamics.\u003c\/p\u003e \u003cp\u003e2.4 Thermodynamically Driven Drug Design.\u003c\/p\u003e \u003cp\u003e2.5 Measurement of Binding Energetics.\u003c\/p\u003e \u003cp\u003e2.6 Structure-based Calculation of Protein Binding Energetics.\u003c\/p\u003e \u003cp\u003e2.7 Interfacial Water Molecules in Protein Recognition.\u003c\/p\u003e \u003cp\u003e2.8 The Linkage Between Binding and Conformational Equilibrium in Proteins.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART II APPROACHES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 On the Logic of Natural Product Binding in Protein-Protein Interactivity\u003c\/b\u003e (\u003ci\u003eJames J. La Clair\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e3.1 Introduction.\u003c\/p\u003e \u003cp\u003e3.2 Structural Logic.\u003c\/p\u003e \u003cp\u003e3.3 Functional Logic.\u003c\/p\u003e \u003cp\u003e3.4 The Need for Programmers.\u003c\/p\u003e \u003cp\u003e3.5 Compiling the NPPI Mapper.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Interface peptide inhibitors of PPIs\u003c\/b\u003e (\u003ci\u003eMark W. Peczuh, and Richard T. Desmond\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e4.1 Interface Peptides Defined.\u003c\/p\u003e \u003cp\u003e4.2 Unmodified Peptides.\u003c\/p\u003e \u003cp\u003e4.3 Modified Peptides.\u003c\/p\u003e \u003cp\u003e4.4 Summary\/Perspective.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5\u003c\/b\u003e \u003cb\u003eInhibition of Protein-Protein Interactions by Peptide Mimics\u003c\/b\u003e (\u003ci\u003eJorge Becerril, Johanna M. Rodriguez, Pauline N. Wyrembak, and Andrew D. Hamilton\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e5.1 Introduction.\u003c\/p\u003e \u003cp\u003e5.2 Inhibition of Calmodulin.\u003c\/p\u003e \u003cp\u003e5.3 Inhibition of HIV-1 Fusion.\u003c\/p\u003e \u003cp\u003e5.4 Inhibition of the Nuclear Estrogen Receptor.\u003c\/p\u003e \u003cp\u003e5.5 Inhibition of the Bcl-x\u003csub\u003eL\u003c\/sub\u003e\/Bak Interaction.\u003c\/p\u003e \u003cp\u003e5.6 Inhibition of the p53\/MDM2 Interaction.\u003c\/p\u003e \u003cp\u003e5.7 Miscellaneous Protein Targets.\u003c\/p\u003e \u003cp\u003e5.8 Conclusion.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6\u003c\/b\u003e \u003cb\u003eDiscovery of Inhibitors of Protein-Protein Interactions by Screening Chemical Libraries\u003c\/b\u003e (\u003ci\u003eCarlos García-Echeverría\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e6.1 Introduction.\u003c\/p\u003e \u003cp\u003e6.2 Screening Strategies to Identify and Develop Antagonists of Protein-Protein Interactions.\u003c\/p\u003e \u003cp\u003e6.3 Mimetics of Common Protein Structure Motifs and Structure-based Design of Peptidomimetics.\u003c\/p\u003e \u003cp\u003e6.4 Conclusions and Outlook.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART III TECHNIQUES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7\u003c\/b\u003e \u003cb\u003eHigh-throughput Methods of Chemical Synthesis Applied to the Preparation of Inhibitors of Protein-Protein Interactions\u003c\/b\u003e (\u003ci\u003eAnnaliese K. Franz, Jared T. Shaw, and Yuchen Tang\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e7.1 Introduction.\u003c\/p\u003e \u003cp\u003e7.2 Survey of High-throughput Organic Synthesis.\u003c\/p\u003e \u003cp\u003e7.3 Synthesis of 'Peptide-Inspired' Compounds and Libraries.\u003c\/p\u003e \u003cp\u003e7.4 Synthesis of 'Natural Product-Inspired' Compounds and Libraries.\u003c\/p\u003e \u003cp\u003e7.5 Diversity Oriented Synthesis (DOS) in the Discovery of PPI Inhibitors.\u003c\/p\u003e \u003cp\u003e7.6 Summary and Outlook.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 \u003ci\u003eIn Silico\u003c\/i\u003e screening\u003c\/b\u003e (\u003ci\u003eF.J. Luque, and Xavier Barril\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e8.1 Introduction.\u003c\/p\u003e \u003cp\u003e8.2 Methods for Virtual Ligand Screening.\u003c\/p\u003e \u003cp\u003e8.3 Binding Site Characterization.\u003c\/p\u003e \u003cp\u003e8.4 Case Studies.\u003c\/p\u003e \u003cp\u003e8.5 Outlook and Conclusions.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9.1\u003c\/b\u003e \u003cb\u003e\u003ci\u003eIn Vitro\u003c\/i\u003e Screening: Screening by Nuclear Magnetic Resonance\u003c\/b\u003e (\u003ci\u003eErnest Giralt\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e9.1.1 Saturation Transfer Difference (STD).\u003c\/p\u003e \u003cp\u003e9.1.2 STD in Fragment-based Drug Design.\u003c\/p\u003e \u003cp\u003e9.1.3 Chemical Shift Perturbation (CSP).\u003c\/p\u003e \u003cp\u003e9.1.4 \u003csup\u003e19\u003c\/sup\u003eF-NMR in Molecular Recognition Studies.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9.2 \u003ci\u003eIn Vitro\u003c\/i\u003e Screening: Methods of High-throughput Screening\u003c\/b\u003e (\u003ci\u003eWenjiao Song and Qing Lin\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e9.2.1 Introduction.\u003c\/p\u003e \u003cp\u003e9.2.2 Statistical Evaluation of the HTS Assay Performance.\u003c\/p\u003e \u003cp\u003e9.2.3 Biochemical Assays.\u003c\/p\u003e \u003cp\u003e9.2.4 Cell-based Assays.\u003c\/p\u003e \u003cp\u003e9.2.5 Conclusion.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART IV CASE STUDIES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Case Study: Inhibitors of the MDM2-p53 Protein-Protein Interaction\u003c\/b\u003e (\u003ci\u003eSanjeev Shangary, Denzil Bernard, and Shaomeng Wang\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e10.1 MDM2-p53 Protein-Protein Interaction: A Case Study.\u003c\/p\u003e \u003cp\u003e10.2 Regulation of p53 by the MDM2-p53 Protein-Protein Interaction.\u003c\/p\u003e \u003cp\u003e10.3 Structural Basis of the MDM2-p53 Interaction.\u003c\/p\u003e \u003cp\u003e10.4 Design of p53-based Peptides.\u003c\/p\u003e \u003cp\u003e10.5 Design of Nonpeptidic Small-Molecule Inhibitors of the MDM2-p53 Interaction.\u003c\/p\u003e \u003cp\u003e10.6 Challenges in the Design of Small Molecule Inhibitors of the MDM2-p53 Interaction.\u003c\/p\u003e \u003cp\u003e10.7 Reactivation of p53 by Inhibitors of the MDM2-p53 Interaction.\u003c\/p\u003e \u003cp\u003e10.8 Development of MDM2 Inhibitors and New Anticancer Drugs.\u003c\/p\u003e \u003cp\u003e10.9 Concluding Remarks.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Case Study: The Discovery of Potent LFA-1 Antagonists\u003c\/b\u003e (\u003ci\u003eTom Gadek\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e11.1 Introduction.\u003c\/p\u003e \u003cp\u003e11.2 Structural, Molecular and Cellular Biologies of LFA-1.\u003c\/p\u003e \u003cp\u003e11.3 The Search for Small Molecule LFA-1 Antagonists.\u003c\/p\u003e \u003cp\u003e11.4 Screening Assays.\u003c\/p\u003e \u003cp\u003e11.5 Lead Identification and Optimization.\u003c\/p\u003e \u003cp\u003e11.6 Protein and Small Molecule Structure Activity Relationships (PSAR) in the LFA-1\/ICAM-1 Interaction.\u003c\/p\u003e \u003cp\u003e11.7 Summary.\u003c\/p\u003e \u003cp\u003eReferences.\u003c\/p\u003e \u003cp\u003eIndex.\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49402275955031,"sku":"9780470059050","price":115.16,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9780470059050.jpg?v=1730479918","url":"https:\/\/bookcurl.com\/products\/protein-surface-recognition-9780470059050","provider":"Book Curl","version":"1.0","type":"link"}