Anmerkung: Intro -- Advances in Carbohydrate Chemistry and Biochemistry -- Copyright -- Contents -- Contributors -- Preface -- Reference -- Chapter One: Mechanism of multivalent glycoconjugate-lectin interaction: An update -- 1. Background and historical perspective -- 2. Mechanism of multivalent lectin binding -- 2.1. Examples and mechanism of intramolecular (face-to-face) binding -- 2.1.1. The asialoglycoprotein receptor -- 2.1.2. Shiga-like toxin and cholera toxin -- 2.1.3. Vancomycin -- 2.2. Examples and mechanism of intermolecular (cross-linking) binding -- 2.2.1. Studies of multivalent glycans binding to lectins ConA and DGL -- 2.2.2. ITC determined n values, structural valency, and functional valency -- 2.2.3. Binding enthalpies increase in direct proportion to the valency of multivalent glycans -- 2.2.4. Binding entropy does not directly increase in proportion to the valency of multivalent glycans -- 2.2.5. The thermodynamic basis for enhanced affinities of multivalent analogs -- 2.2.6. The epitopes of a multivalent glycan possess a gradient of decreasing microscopic affinity constants -- 2.3. Binding of lectins to multivalent mucins -- 2.3.1. Mucins: Glycoproteins that are heavily O-glycosylated -- 2.3.2. The mechanism of lectin-mucin interaction -- 2.3.3. Affinity of lectin-mucin interaction is proportional to the length of mucins -- 2.3.4. Mechanisms of binding of lectins to mucins: The ``bind-and-jump´´ model -- 2.4. Multivalent interactions between lectins and globular glycoproteins -- 2.5. Multivalency of glycosaminoglycans (GAGs) and proteoglycans (PGs) -- 2.5.1. Glycosaminoglycans (GAGs) and proteoglycans (PGs) engage in multivalent interactions with human galectin-3 (Gal-3) -- 2.5.2. CSA and CSC, not heparin and CSB, are multivalent ligands of Gal-3. , 2.5.3. Affinity of Gal-3 depends on the chain length of GAGs: The ``bind and jump´´ mechanism -- 2.6. Scaffolds of glycoconjugates play crucial roles in multivalent interactions -- 2.6.1. Scaffolds provide physical platforms to which glycan chains are covalently linked -- 2.6.2. Lectin binding entropy becomes more favorable when a free glycan is covalently attached to a protein scaffold -- 2.6.3. Structures of protein scaffolds may limit glycan density-dependent affinity effects -- 2.6.4. Entropic advantage of glycosylation -- 2.6.5. Scaffolds of glycoconjugates play a regulatory role in the kinetics of lattice formation -- 2.6.6. Scaffolds can diversify the functions of glycoconjugates and their binding partners (lectins) -- 2.6.7. Beyond affinity and valence effects -- 2.7. Multivalency and non-covalent cross-linking -- 2.7.1. Binding of multivalent glycoconjugates/glycans to oligomeric lectins leads to the formation of non-covalent crossl ... -- 2.7.2. The structures of the multivalent glycans and lectins determines their cross-linking properties -- 3. Current and future challenges -- 4. Concluding remarks -- Acknowledgments -- References -- Chapter Two: Multivalent lectin-carbohydrate interactions: Energetics and mechanisms of binding -- 1. Introduction -- 2. Mucins: Background -- 3. Binding of lectins to mucins -- 3.1. Affinities of SBA and VML for mucins -- 3.2. Thermodynamics of SBA binding Tn-PSM -- 3.3. Thermodynamics of SBA binding 81-mer Tn-PSM -- 3.4. Thermodynamics of SBA binding 38/40-mer Tn-PSM -- 3.5. Thermodynamics of SBA binding Fd-PSM -- 3.6. Thermodynamics of VML binding Tn-PSM -- 3.7. Thermodynamics of VML binding 81-mer Tn-PSM and 38/40-mer Tn-PSM -- 3.8. Thermodynamics of VML binding Fd-PSM -- 4. Mechanisms of binding of SBA and VML to PSM: The bind and jump model -- 5. Thermodynamics of lectin-mucin cross-linking interactions. , 5.1. Hill plots show evidence of increasing negative cooperativity -- 5.2. Analysis of the stoichiometry of binding of SBA to the mucins -- 5.3. Cross-linking of lectins with the mucins correlate with decreasing favorable entropy of binding -- 6. Conclusions and perspective -- 6.1. The bind and jump model for lectin-mucin interactions -- 6.2. Implications of increasing negative cooperativity and decreasing favorable binding entropy of lectins-mucin cross-li ... -- References -- Author index -- Subject index.