Multivalency

Jurriaan Huskens, PhD (1968) is full professor of "Molecular Nanofabrication" at the University of Twente, Netherlands. Present research interests encompass: supramolecular chemistry at interfaces, supramolecular materials, multivalency, nanofabrication, and solar fuels. Leonard J. Prins, PhD is a professor in Organic Chemistry at the University of Padova, Italy. His current research interests include network reactivity in complex chemical systems and the origin of cooperativity in multivalent catalysts. Rainer Haag, PhD joined the Freie Universität Berlin as full Professor of Organic and Macromolecular Chemistry in 2004. Currently he serves on the Editorial Board of the Angewandte Chemistry and is the spokesperson of the collaborative research center 765 on "multivalency." Bart Jan Ravoo, PhD (1970) is full professor at the Westfälische Wilhelms-Universität Münster, Germany, where he is in charge of the "Synthesis of Nanoscale Systems" group. Since 2016 he is co-director of the Center for Soft Nanoscience (SoN). His main research interest are soft materials made by self-assembly, functional nanoparticles, and self-assembled monolayers.

• List of Contributors xiForeword xvPreface xviiPart I General Introduction to Multivalent Interactions 11 Additivity of Energy Contributions in Multivalent Complexes 3Hans-Jorg Schneider1.1 Introduction 31.2 Additivity of Single Interactions – Examples 31.3 Limitations of Additivity 71.3.1 Free Energy Values ΔG Instead of Enthalpic and Entropic Values ΔH, TΔS 71.3.2 Mismatch as Limitation of Additivity 91.3.3 Medium Effects as Limiting Factor 121.3.4 Strain and Induced Fit 121.4 Cooperativity 131.5 Allostery 141.6 Conclusions 17References 182 Models and Methods in Multivalent Systems 23Jurriaan Huskens2.1 Introduction 232.1.1 General Introduction 232.1.2 Multivalent versus Cooperative Interactions 242.2 Numerical Data Analysis 252.2.1 Model Simulations Using a Spreadsheet Approach 262.2.2 Setting Up and Assessing Titrations 302.2.3 Using Spreadsheet Simulations to Fit Experimental Data to a Model 362.3 Models for Multivalent Systems 412.3.1 The Simplest Multivalent System: A 1:1 Complex with Two Interaction Sites 412.3.2 Multivalent Binding at Surfaces 462.4 Special Multivalent Systems 532.4.1 Increasing the Valency of Interfacial Assemblies: Dendrimers, Oligomers, and Polymers  532.4.2 Heterotropic Interactions 582.4.3 Kinetics and Dynamics 632.5 Conclusions 68Acknowledgments 68References 683 Design Principles for Super Selectivity using Multivalent Interactions 75Tine Curk, Jure Dobnikar, and Daan Frenkel3.1 Introduction 753.1.1 Background: Ultra-sensitive Response 753.2 Super Selectivity: An Emergent Property of Multivalency 783.3 Multivalent Polymer Adsorption 843.4 Which Systems are Super Selective? 863.4.1 Rigid Geometry Interactions 863.4.2 Disordered Multivalency 873.5 Design Principles for Super-Selective Targeting 903.6 Summary: It is interesting, but is it useful? 93Appendix 3.A: What Is Effective Molarity? 95Acknowledgements 98References 984 Multivalency in Biosystems 103Jens Dernedde4.1 Introduction 1034.2 Cell–Cell Adhesion 1044.2.1 Homotypic Interactions, Cadherins Keep Cells Together 1054.2.2 Selectins, Heterotypic Cell Adhesion to Fight Infections 1064.2.3 Bacterial Adhesion by FimH 1084.3 Phase Transition, Multivalent Intracellular Assemblies 1094.4 Multivalency in the Fluid Phase, Pathogen Opsonization 1114.5 Conclusion 113Acknowledgment 113References 114Part II Multivalent Systems in Chemistry 1215 Multivalency in Cyclodextrin/Polymer Systems 123Akihito Hashidzume and Akira Harada5.1 Introduction 1235.2 General Perspectives of Multivalency in Cyclodextrin/Polymer Systems 1255.3 Typical Examples of Multivalency in Cyclodextrin/Polymer Systems 1265.3.1 Formation of Polymer Aggregates from Cyclodextrin-Polymers and Guest-Polymers 1265.3.2 Selectivity of Interaction Enhanced by Multivalency 1275.3.3 Self-Healable Hydrogels Based on Multivalency 1345.4 Summary and Outlook 136Acknowledgments 136References 1386 Cucurbit[n-uril-Mediated Multiple Interactions 143Zehuan Huang and Xi Zhang6.1 Introduction to Cucurbit[n-uril Chemistry 1436.2 Heteroternary Complexes 1436.3 Homoternary Complexes 1466.4 Conclusions 150References 1507 Multivalency as a Design Criterion in Catalyst Development 153Paolo Scrimin, Maria A. Cardona, Carlos M. Leon Prieto, and Leonard J. Prins7.1 Introduction 1537.2 Formation of Enzyme-Like Catalytic Pockets 1547.3 Cooperativity Between Functional Groups 1577.4 Mechanistic Effects 1617.5 The Dendritic Effect in Multivalent Nanozymes 1647.5.1 Peptide-Based Dendrimers for the Cleavage of Phosphodiesters 1667.5.2 Catalytic 3D SAMs on Au NPs 1687.6 Multivalent Catalysts and Multivalent Substrates 1707.7 Conclusions 172Acknowledgements 174References 1748 Multivalent Molecular Recognition on the Surface of Bilayer Vesicles 177Jens Voskuhl, Ulrike Kauscher, and Bart Jan Ravoo8.1 Introduction 1778.2 Molecular Recognition of Vesicles 1798.2.1 Metal Coordination 1808.2.2 Light Responsive Interactions 1848.2.3 Hydrogen Bonding and Electrostatic Interactions 1858.3 Biomimetic Vesicles 1888.3.1 Vesicles as Multivalent Platforms 1888.3.2 Membrane Fusion 1938.4 Vesicle-based Supramolecular Materials 1968.4.1 Hydrogels 1968.4.2 Immobilization of Vesicles 1988.4.3 Nanoparticles and Nanocontainers 1988.5 Conclusion 201Acknowledgment 201References 201Part III Multivalent Systems in Biology 2059 Blocking Pathogens by Multivalent Inhibitors 207Sumati Bhatia, Benjamin Ziem, and Rainer Haag9.1 Introduction 2079.2 Design of Multivalent Ligand Architectures 2099.3 Multivalent Carbohydrate Ligands 2129.4 Scaffold Architecture 2159.4.1 Linear and Dendritic Scaffolds 2159.4.2 Multivalent Gold Nanoparticles 2189.4.3 2D Platforms 2209.5 Nano-and Microgels for Pathogen Inhibition 2229.6 Conclusion 223Acknowledgments 224References 22410 Multivalent Protein Recognition Using Synthetic Receptors 229Akash Gupta, Moumita Ray, and Vincent M. Rotello10.1 Introduction 22910.2 Structural Properties of Protein Surfaces 22910.2.1 Protein–Protein Interfacial Areas 22910.2.2 Chemical Nature of the Protein–Protein Interface 23010.2.3 “Hot Spots” 23010.2.4 O-Ring Structure 23210.3 Synthetic Receptors for Protein Surface Recognition 23210.3.1 Porphyrin Scaffolds for Protein Surface Recognition 23210.3.2 Protein Surface Recognition Using Molecular Tweezers 23810.3.3 Calixarene Scaffolds for Protein Surface Recognition 24010.3.4 Recognition of Protein Surfaces Using Nanoparticles 24310.3.4.1 Nanoparticles as Protein Mimics 24410.3.4.2 Regulating the Structure and Function of Proteins Using Nanoparticles 24610.3.4.3 Nanoparticle-based Protein Sensors 25010.4 Future Perspective and Challenges 254Acknowledgment 257References 25711 Multivalent Calixarenes for the Targeting of Biomacromolecules 263Francesco Sansone and Alessandro Casnati11.1 Introduction 26311.2 Binding to Proteins and Enzymes 26611.3 Recognition of Carbohydrate Binding Proteins (Lectins) 27311.4 Binding Polyphosphates, Oligonucleotides and Nucleic Acids 27911.5 Conclusions 284Acknowledgements 285References 28512 Cucurbit[n]uril Assemblies for Biomolecular Applications 291Emanuela Cavatorta, Luc Brunsveld, Jurriaan Huskens, and Pascal Jonkheijm12.1 Introduction 29112.2 Molecular Recognition Properties of CB[n- 29312.2.1 Interactions with the Carbonyl Portals of CB[n- 29312.2.2 Release of High Energy Water Molecules from the CB[n- Cavity 29512.2.3 Enthalpy-driven Hydrophobic Effect for CB[n- 29512.2.4 Enthalpy-driven Hydrophobic Effect for CB[8- Heteroternary Complexes 29712.3 Control Over the Binding Affinity with CB[n- 29912.4 CB[n] Recognition of Amino Acids, Peptides, and Proteins 30112.5 CB[n] for Bioanalytical and Biomedical Applications 30512.5.1 CB[n]-mediated Assembly of Bioactive Polymers and Hydrogels 30512.5.2 CB[n]-mediated Assembly of Bioactive Nanoparticles 30712.5.3 CB[n]-mediated Assembly on Bioactive Surfaces 31312.6 Conclusions and Outlook 317Acknowledgment 319References 31913 Multivalent Lectin–Glycan Interactions in the Immune System 325Joao T. Monteiro and Bernd Lepenies13.1 Introduction 32513.2 Targeting Innate Immunity to Shape Adaptive Immunity 32713.3 C-type Lectin Receptors 32813.3.1 Multivalent Glycoconjugates Targeting DC-SIGN 33113.3.2 Multivalent Glycoconjugates Targeting Other CLRs 33113.4 Galectins 33213.5 Siglecs 33413.6 Conclusions 335Acknowledgment 335References 33514 Blocking Disease Linked Lectins with Multivalent Carbohydrates 345Marjon Stel and Roland J. Pieters14.1 Introduction 34514.2 Haemagglutinin 34714.3 LecA 34914.4 LecB 35414.5 Galectins 35814.6 Concanavalin A 36214.7 Cholera Toxin 36614.8 Propeller Lectins 36714.9 Conclusion 371Acknowledgements 371References 371Index 381