Intro -- Contents -- Preface -- Section 1: Chemical Principles in Drug Design and Discovery -- 1.1 Functional Groups of Biomolecules and their Reactions -- 1.1.1 Functional Groups in Biological Systems -- 1.1.2 Acids and Bases Versus Electrophiles and Nucleophiles -- 1.1.3 Stereoisomerism and Chirality -- 1.1.3.1 Cis/trans Isomerism -- 1.1.3.2 Chirality and Enantiomerism -- 1.1.4 Common Mechanisms in Biological Chemistry -- 1.1.4.1 Nucleophilic Substitution Reactions -- 1.1.4.1.1 SN2 - Bimolecular Nucleophilic Substitution -- 1.1.4.1.2 SN1 ‒ Unimolecular Nucleophilic Substitution Reactions -- 1.1.4.1.3 Phosphate Group Transfer - the Grey Area of Nucleophilic Substitutions in Biological Syste -- 1.1.4.2 Electrophilic Addition Reactions -- 1.1.4.2.1 Synthesis of (Sa(B-Terpineol ‒ Intramolecular Addition -- 1.1.4.3 Aromatic Substitutions -- 1.1.4.3.1 Electrophilic Aromatic Substitution -- 1.1.4.3.2 Nucleophilic Aromatic Substitutions -- 1.4.3.3 Hallucinogen Synthesis ‒ Aromatic Substitution on Fungi -- 1.4.4 Eliminations Reactions -- 1.1.4.4.1 E1 ‒ Unimolecular Elimination -- 1.1.4.4.3 E1cB ‒ Unimolecular Elimination through Conjugate Base -- 1.1.4.5 Nucleophilic Carbonyl Addition Reactions -- 1.1.4.5.1 Nitrofurantoin ‒ a Semicarbazone -- 1.1.1.4.6 Acyl Substitution Reactions -- 1.1.4.6.1 Aspirin ‒ Esterifications and Transesterifications -- 1.1.1.4.7 Carbonyl Condensation Reactions -- 1.1.4.7.1 Aldol Reaction -- 1.1.4.7.2 Claisen Condensation -- 1.1.4.7.3 Aldolases ‒ Stabilization Strategies -- 1.1.4.8 Oxidations and Reductions -- 1.1.4.8.1 Disulfide Bridges ‒ Oxidized Thiols -- 1.1.5 The Organic Mechanisms of Biological Transformations -- 1.1.5.1 Cis/trans-Isomers Interconversion in the Vision Pathway -- 1.1.5.2 Metabolism of Fatty Acids ‒ (Sb(B-Oxidation Pathway -- 1.1.5.3 Penicillin ‒ a Strong Acylating Agent.

1.1.5.3.1 Transpeptidase Mechanism -- 1.1.5.3.2 Transpeptidase Inhibition -- 1.1.5.3.3. Penicillin Biosynthesis -- 1.1.5.4 NAD+ − a Classical Coenzyme -- 1.1.5.5. FAD − a More Versatile Coenzyme -- 1.1.5.6 Biotin and Carboxylation Reactions -- References -- 1.2 Designing Covalent Inhibitors: A Medicinal Chemistry Challenge -- 1.2.1 Introduction -- 1.2.2 Designing Safer Covalent Inhibitors -- 1.2.3 Case Study 1: Michael Acceptors to Treat Infectious Diseases -- 1.2.3.1 K777 Inhibitor -- 1.2.3.2 Rupintrivir (AG7088) -- 1.2.4 Case Study 2: From Covalent Inhibitors to Hybrid Drugs -- 1.2.4.1 Hybrid Compounds Containing an Electrophilic Warhead -- 1.2.4.2 Hybrid Compounds Containing a Masked Electrophilic Warhead -- 1.2.5 Conclusions -- References -- Section 2: Chemical Basis of Drug Action and Diseases -- 2.1 Pharmacokinetics and Bioanalysis to Improve Drug Development -- Abbreviations -- 2.1.1 Introduction -- 2.1.2 Pharmacokinetics on Drug Discovery and Development Process -- 2.1.2.1 ADME/Pharmacokinetic Evaluation on Early Drug Discovery Phases -- 2.1.2.2 Pharmacokinetic Evaluation on Drug Development Phases -- 2.1.3 Bioanalysis and Validation Requirements on DDD -- 2.1.4 Bioanalysis &amp -- Pharmacokinetics, a Synergistic Partnership on DDD -- 2.1.4.1 Bioanalytic Support of In Vitro ADME Studies -- 2.1.4.2 Bioanalytic Support of In Vivo ADME/Pharmacokinetic Studies -- 2.1.5 Conclusions -- References -- 2.2 Translational Research in Endocrinology and Neuroimmunology Applied to Depression -- 2.2.1 Major Depressive Disorder -- 2.2.2 The Stress Response -- 2.2.2.1 The CRH System and the Stress Response -- 2.2.2.2 The Locus Ceruleus Norepinephrine (LC-NE) System and Other Central Nervous System (CNS) Stru -- 2.2.2.3 The Immune System -- 2.2.3 The Effect of Chronic Stress and MDD in Dysregulating the Core Stress System.

2.2.4 Summary and Conclusions -- References -- 2.3 Understanding the Metabolic Syndrome Using a Biomedical Chemistry Profile -- 2.3.1 Introduction -- 2.3.2 Natural Mineral-rich Waters and MetSyn -- 2.3.3 Magnesium and MetSyn/MetSyn Features - Associated Mechanisms -- 2.3.4 Calcium and MetSyn/MetSyn Features - Associated Mechanisms -- 2.3.5 Potassium and MetSyn/MetSyn Features - Associated Mechanisms -- 2.3.6 Bicarbonate and MetSyn/MetSyn Features - Associated Mechanisms -- 2.3.7 Magnesium, Calcium, Potassium and Bicarbonate versus Sodium -- 2.3.8 Conclusion -- References -- 2.4 Brain Neurochemistry and Cognitive Performance: Neurotransmitter Systems -- 2.4.1 Monoaminergic Neurotransmission and Cognition -- 2.4.2 Glutamate Neurotransmission and Cognition -- 2.4.3 GABAergic Neurotransmission and Cognition -- 2.4.4 Gliotransmitters -- 2.4.5 Cognitive Enhancement -- References -- Section 3: Strategies to Develop New and Better Drugs -- 3.1 Amino Acids and Peptides in Medicine: Old or New Drugs? -- 3.1.1 Introduction -- 3.1.1.1 Amino acids: biological and chemical concepts -- 3.1.2 Amino Acids and Drug Development -- 3.1.2.1 Rationale for Drug Design -- 3.1.2.2 Amino Acid Prodrug in Drug Delivery -- 3.1.2.3. L-type Amino Acid Transporter -- 3.1.2.4. Variability of Amino Acid Application to Exclusive Drugs -- 3.1.3 Peptides for Biomedicine -- 3.1.3.1 Antimicrobial Peptides (AMPs) -- 3.1.3.1.1 AMPs: Mechanism of Action and Peptide Families -- 3.1.3.1.2 (Sa(B-Helical Peptides without Cys Residues -- 3.1.3.1.3 Peptides Containing Disul de Bridges -- 3.1.3.1.4 Peptides Rich in Pro, Gly, His, Arg and Trp Residues -- 3.1.3.3 Peptides: Scaffolding Materials in Tissue Engineering -- 3.1.3.3.1 Peptide-based Biopolymers -- 3.1.3.3.2 Strategies to Create Scaffolds as Instructive Extracellular Microenvironments for Tissue E.

3.1.3.3.3 Peptide-based Biomaterials Responsive to Environmental Cues -- 3.1.3.3.4 Self-assembling Peptides as Biomaterials -- 3.1.3.4 Therapeutic Peptides and Market -- 3.1.3.4.1 Chemical Strategies to Improve Peptide Biological Activity -- 3.1.3.4.2 Market -- 3.1.4 Conclusions -- References -- 3.2 Targeting Calcium-mediated Excitotoxicity in the CNS -- 3.2.1 Introduction -- 3.2.2 Glutamate and Glutamate Receptors -- 3.2.2.1 AMPA Receptors -- 3.2.2.2 Kainate Receptors -- 3.2.2.3 NMDA Receptors -- 3.2.3 The Role of Calcium in Normal Neuronal Biochemistry -- 3.2.4 Excitotoxicity -- 3.2.5 The Role of Calcium in Excitotoxic Neuronal Biochemistry -- 3.2.6 Diseases that are Potentially Exacerbated by Calcium-mediated Excitotoxicity -- 3.2.6.1 Amyotrophic Lateral Sclerosis (ALS) -- 3.2.6.2 Multiple Sclerosis (MS) -- 3.2.6.3 Alzheimer's Disease (AD) -- 3.2.6.4 Huntington's Disease (HD) -- 3.2.6.5 Stroke -- 3.2.6.6 Parkinson's Disease -- 3.2.6.7 Traumatic Brain or Spinal Cord Injury -- 3.2.7 Why not Fully Block Calcium Entry via Pharmacological Agents? -- 3.2.8 Emerging Targets for Reducing Calcium-mediated Excitotoxicity -- 3.2.9 Conclusions and Outlook -- References -- 3.3 Strategies for Conversion of Peptides to Peptidomimetic Drugs -- 3.3.1 Peptides as Starting Points in Drug Discovery -- 3.3.1.1 Strategy for the Development of Peptidomimetics -- 3.3.1.1.1 Property Elucidation -- 3.3.1.1.2 Structure-Activity Relationship -- 3.3.1.1.3 Bioactive Conformation -- 3.3.1.1.3.1 Secondary Structure Mimetics -- 3.3.2 A Case study of Rational Peptide Lead Optimization: Development of Small and Constrained Pepti -- 3.3.2.1 SP1-7 and its Binding Site -- 3.3.2.2 SAR and Truncation Studies of SP1-7 and EM-2 -- 3.3.2.2.1 Strategy -- 3.3.2.2.2 Structure-activity Relationship -- 3.3.2.2.3 Effects of SP1-7 and its Analogs.

3.3.2.3 Design and Synthesis of Small Constrained H-Phe-Phe-NH2 Analogs -- 3.3.2.3.1 Strategy -- 3.3.2.3.2 Structure-activity relationship and ADME properties -- 3.3.3 Conclusion -- References -- 3.4 Synthetic Vs. Natural Bioactive Compounds Against Tropical Disease -- 3.4.1 Introduction -- 3.4.2 Early History of Malaria Treatment -- Quinine and Artemisinin -- 3.4.3 Post World War II and the Development of Synthetic Anti-malarials -- 3.4.4 Modern Efforts in Antimalarial Drug Development -- 3.4.4.1 Quinine, 4-Aminoquinolines, and Quinoline Methanols -- 3.4.4.2 8-Aminoquinolines -- 3.4.4.3 Artemisinins and other Endoperoxides -- 3.4.4.4 Repurposed Drugs -- 3.4.5 Natural Products in the Treatment of Malaria -- 3.4.6 Considerations for Anti-parasitic Drug Development -- References -- 3.5 Current Trends and Developments for Nanotechnology in Cancer -- 3.5.1 Introduction -- 3.5.2 Drug Delivery Nanosystems in Cancer Therapy -- 3.5.2.1 Controlled Drug Delivery -- 3.5.2.2 Stimuli-responsive Controlled Drug Delivery Systems -- 3.5.2.3 Combination Therapy -- 3.5.3 Cancer Targeting -- 3.5.3.1 Passive Targeting -- 3.5.3.1.1 The Fundamentals of Passive Targeting and the EPR Effect -- 3.5.3.1.2 Physicochemical Properties of Nanoparticles Affecting the Passive Targeting -- 3.5.3.1.3 Challenges and Future Prospects of Passive Targeting -- 3.5.3.2 Active Targeting -- 3.5.3.2.1 The Fundamentals of Active Targeting -- 3.5.3.2.2 Factors Affecting Tumor Active Targeting -- 3.5.3.2.3 Ligands for Tumor Active Targeting -- 3.5.3.2.3.1 Monoclonal Antibodies -- 3.5.3.2.3.2 Proteins and Peptides -- 3.5.3.2.3.3 Aptamers -- 3.5.3.2.3.4 Small Molecules -- 3.5.4 Nanotechnology and Immunotherapy -- 3.5.4.1 Nano-based Cancer Immunotherapy -- 3.5.4.2 Nanoparticulate Adjuvants for Cancer Immunotherapy -- 3.5.4.3 Nanoparticle Based DC Targeting for Cancer Immunotherapy.

3.5.5 Cancer Imaging, Diagnostics and Multifuctional Nanosystems.

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Electronic reproduction. Ann Arbor, Michigan : ProQuest Ebook Central, 2022. Available via World Wide Web. Access may be limited to ProQuest Ebook Central affiliated libraries.