Natural Products as Enzyme Inhibitors: An Industrial Perspective

Preface
Contents
About the Editors
Chapter 1: Fourth-Generation Allosteric EGFR Tyrosine Kinase Inhibitors to Combat the Drug Resistance Associated with Non-smal...
	1.1 Introduction
	1.2 EGFR Tyrosine Kinase Allosteric Binding Site
	1.3 Allosteric Inhibitors
	1.4 Conclusion and Future Perspectives
	References
Chapter 2: Plant Peptides as Protease Inhibitors for Therapeutic and Agricultural Applications
	2.1 Introduction
	2.2 Plant Protease Inhibitors: Defensive Function
		2.2.1 Serine PIs
		2.2.2 Kunitz-Type Serine PIs: Diverse and Sometimes Can be Multifunctional
		2.2.3 Bowman-Birk-Type Serine PI: Smaller but Strong
		2.2.4 Potato Type I and II Serine PIs: Inducible and Multidomain
		2.2.5 Cereal-Type Serine PI: Poaceae Specific and Bifunctional
		2.2.6 Squash-Type Serine PIs: Cucurbitaceae Specific, Small, Highly Stable, and Strong
		2.2.7 Mustard-Type Serine PI: Cruciferous Specific and Special
		2.2.8 Cysteine PIs: From Diverse Plant Species with Endogenous Function
		2.2.9 Aspartate PIs
		2.2.10 Metalloprotease PIs: Rare but Unique
	2.3 Short Peptides as PIs
		2.3.1 Cyclotides
		2.3.2 Orbitides
		2.3.3 Lyciumin
		2.3.4 SFTI-1-Related Peptides (PawS-Derived Peptides)
		2.3.5 Defensins
	2.4 Synthetic Peptides Engineered from Plant Proteins
		2.4.1 Engineering of Cyclotides
		2.4.2 SFTI Analogues
		2.4.3 BBI Reactive Loop Engineering
		2.4.4 Pin-II PI Reactive Loop Engineering
	2.5 Agricultural and Therapeutic Applications of PI Peptides
		2.5.1 Agricultural Applications
		2.5.2 Therapeutic Applications
	2.6 Synthesis and Production of Plant Peptides
	2.7 Conclusion and Future Perspectives
	References
Chapter 3: Bioactive α-Amylase Inhibitors: Sources, Mechanism of Action, Biochemical Characterization, and Applications
	3.1 Introduction
	3.2 Amylases
		3.2.1 Forms of Amylases
		3.2.2 Structural Characteristics of Amylases
		3.2.3 Distribution and Significance of Amylases
		3.2.4 Problems Associated with Highly Active Amylases
	3.3 α-Amylase Inhibitors (α-AIs)
	3.4 Sources of α-AIs
	3.5 Classification of α-AI
		3.5.1 Non-proteinaceous α-AI
		3.5.2 Proteinaceous α-AIs
	3.6 Mechanism of Interaction of α-AIs with Amylases
	3.7 Extraction and Purification Strategies for α-AI
	3.8 Biochemical Characteristics of α-AIs
		3.8.1 Temperature and pH Stability
		3.8.2 Kinetic Behavior
		3.8.3 Glycoprotein Nature
	3.9 Allelic Variants of AIs from the Same Species
	3.10 Biological Applications of α-AIs
		3.10.1 Pesticidal Applications of α-AIs
		3.10.2 Antimicrobial Activity of α-AIs
		3.10.3 Human Health Management Related Applications of α-AI
		3.10.4 Food Processing Industrial Application of α-AI
	3.11 Limitations of α-AIs to Be Used as Dietary Source Protein for Mammals
	3.12 Scope of Amylase Inhibitor Research
	3.13 Conclusion and Future Perspective of α-AI Research
	References
Chapter 4: Recent Updates on In Silico Screening of Natural Products as Potential Inhibitors of Enzymes of Biomedical and Phar...
	4.1 Introduction
	4.2 Molecular Docking with AutoDock
		4.2.1 Computational Tools Required for Docking
			4.2.1.1 Starting with a Set of Preliminary and Important Requirements
			4.2.1.2 Download the PDB (Protein Data Bank) File
			4.2.1.3 Download the Computational Tools
				AutoDock 4.2.6
				MGL/AutoDockTools
				Method-Docking Approach
		4.2.2 Preparation of Protein for Autodock
		4.2.3 Preparation of Ligand for Autodock
		4.2.4 Docking Approach
			4.2.4.1 Preparation of Grid Parameter File (GPF)
			4.2.4.2 Preparation of Docking Parameter File (DPF)
			4.2.4.3 Running AutoGrid4 and AutoDock4
			4.2.4.4 Analyzing Docking Results
	4.3 Significance of Molecular Docking in Inhibitor Screening for Biomedical Applications
	4.4 Limitations of Molecular Docking
	References
Chapter 5: H+/K+-ATPase Inhibitors from Plants: A Potential Source for Drug Discovery
	5.1 Introduction
	5.2 Structure of Gastric H+/K+-ATPase and Its Role as a Drug Target
	5.3 Mechanism of Action of H+/K+-ATPase Inhibitors
	5.4 Plant Nutraceutical Products as Proton Pump Inhibitors
	5.5 Nutraceuticals Compounds as Proton Pump Inhibitors
	5.6 Conclusion
	References
Chapter 6: Use of Protease Inhibitors as a Promising Alternative for Pest Control
	6.1 Introduction
	6.2 Serine Proteases and Plant Protease Inhibitors
	6.3 Contributions in the Field from Our Research Group
	6.4 Final Considerations
	References
Chapter 7: Pancreatic Lipase (PL) Inhibitors from Medicinal Plants and Their Potential Applications in the Management of Obesi...
	7.1 Introduction
		7.1.1 Mechanism of Obesity and Pancreatic Lipases
		7.1.2 Pancreatic Lipases
		7.1.3 Mechanism of Action of PL Inhibitors
	7.2 PL Inhibitors and Anti-obesity Regime
	7.3 Natural Products as PL Inhibitors
	7.4 Contributions in the Field from Our Research Group
	7.5 Conclusion
	References
Chapter 8: Bioactive Peptides and Polysaccharides: Setting a New Trend in Replacing Conventional Angiotensin-Converting Enzyme...
	8.1 Introduction
	8.2 Sources of ACE Inhibitory Polysaccharides and Peptides
		8.2.1 Polysaccharides
		8.2.2 Peptides
	8.3 Extraction and Identification of ACE Inhibitory Polysaccharides and Peptides
		8.3.1 Polysaccharides
		8.3.2 Peptides
	8.4 Inhibition Mechanism of ACE Inhibitory Polysaccharides and Peptides
		8.4.1 Polysaccharides
		8.4.2 Peptides
	8.5 Consideration in Choosing ACE Inhibitory Polysaccharides/Peptides
	References
Chapter 9: Natural Protease Inhibitors and Their Therapeutic Potentials Against SARS-CoV-2
	9.1 Introduction
	9.2 Viral Proteases and Their Role in the Pathogenesis
	9.3 Natural Inhibitors of Mpro Proteins
		9.3.1 Plant-Based Inhibitors of Mpro
		9.3.2 Phytochemicals with Mpro Inhibitory Activity
			9.3.2.1 Flavonoids
			9.3.2.2 Coumarin
			9.3.2.3 Alkaloids and Terpenoids
		9.3.3 Microbial Products as Inhibitors of Mpro
	9.4 Conclusion
	References
Chapter 10: Telomerase and its Inhibitor in Cancer Therapeutics: Current Status and Future Prospective
	10.1 Introduction
	10.2 Telomerase: The Anti-Aging Enzyme
	10.3 Mechanism of Action of Telomerase
	10.4 Telomerase: A Critical Hallmark of Cancer
	10.5 Identification of Cancer Cells
	10.6 Telomerase Inhibitors
		10.6.1 AZT: Inhibitor of Reverse Transcriptase
		10.6.2 Natural Telomerase Inhibitors (NTI)
			10.6.2.1 Inhibitors Targeting hTERT
			10.6.2.2 hTERT Immunotherapy
			10.6.2.3 Antisense against hTR and hTERT
		10.6.3 Altering Telomerase Activity to Induce Telomeric Dysfunction, which Causes Cancer Cell Death
		10.6.4 Antagonist Template to hTR (RNA Template of Telomerase)
		10.6.5 Combination Therapies
		10.6.6 Cisplatin in Cancer Therapy
		10.6.7 Mode of Action
		10.6.8 Cisplatin and Primary Hepatocellular Carcinoma (PHCC)
		10.6.9 Cisplatin and Lung Cancer
	10.7 Conclusion
	References
Chapter 11: Metal Nanomaterials as Enzyme Inhibitors and Their Applications in Agriculture and Pharmaceutics
	11.1 Introduction
	11.2 Potential of a Metal Nanomaterial as an Enzyme Inhibitor
	11.3 Nanoparticles Inhibiting Vital Enzymes (Some Examples)
	11.4 Future of Nanoparticles as an Enzyme Inhibitor
		11.4.1 Nanoparticles as Protease Inhibitors in Pest Management
		11.4.2 Nano Metals as Urease Inhibitors
	11.5 Conclusion
	References
Chapter 12: α-Glucosidase Inhibitors for Diabetes/Blood Sugar Regulation
	12.1 Introduction
	12.2 Digestive Enzymes Targeted for Diabetes
		12.2.1 Alpha-Amylase
		12.2.2 Alpha-Glucosidase
		12.2.3 Insulin
	12.3 Oral Agents for Diabetes
	12.4 Alpha-Glucosidase Inhibitors for Diabetes
	12.5 Mechanism of Action of Alpha-Glucosidase Inhibitors
	12.6 Alpha-Glucosidase Inhibitors in the Market
	12.7 Side Effects Caused by Alpha-Glucosidase Inhibitors
	12.8 Conclusion
	References