Biologically Active Peptides: From Basic Science to Applications for Human Health

Front Cover
Biologically Active Peptides
Copyright Page
Contents
List of contributors
Preface
1 Bioactive peptides in health and disease: an overview
1.1 Introduction
1.2 Preparation of bioactive peptides
1.3 Absorption of peptides in the small intestine
1.3.1 Paracellular transport
1.3.2 Transcellular transport
1.3.3 Absorption of peptides in the large intestine (colon)
1.3.4 Approaches for enhancing the absorption of peptides
1.3.5 Structure-activity relationship of bioactive peptides
1.4 Bioactivities of food-derived bioactive peptides focusing on inhibiting chronic diseases
1.4.1 Anticancer activity
1.4.2 Anti-inflammatory effect
1.4.3 Antimicrobial activity
1.4.4 Antihypertensive effect
1.4.5 Immunomodulatory peptides
1.4.6 Antidiabetic effect
1.5 Conclusion
References
2 Enzymatic mechanisms for the generation of bioactive peptides
2.1 Introduction
2.1.1 Enzymatic mechanisms in the hydrolysis of food proteins
2.1.2 Bioactive peptides generated during food processing
2.1.3 Bioactive peptides generated through the hydrolysis of proteins with commercial peptidases
2.2 Degree of hydrolysis
2.2.1 Definition
2.2.2 Precursor techniques and alternative methods/procedures
2.3 Assay of endopeptidase activity
2.3.1 Definition
2.3.1.1 Materials, equipment, and reagents
2.3.1.2 Protocol
2.3.1.3 Analysis
2.3.1.4 Alternative methods/procedures
2.4 Assay of exopeptidase activity
2.4.1 Definition
2.4.2 Materials, equipment, and reagents
2.4.3 Protocol
2.4.3.1 Analysis
2.4.3.2 Alternative methods/procedures
2.4.4 Pros and cons
2.4.5 Summary
References
3 Novel technologies in bioactive peptides production and stability
3.1 Introduction
3.2 Expression of recombinant peptides
3.2.1 Escherichia coli expression vectors and strains for recombinant protein production
3.3 Stability of proteins and peptides
3.4 Definition: production of recombinant bioactive peptides in Escherichia coli
3.4.1 Antihypertensive peptides
3.4.2 Antiangiogenic peptides
3.5 Protocol
3.5.1 Antihypertensive cassette design
3.5.2 Amplification of the encrypted vasoinhibin peptide
3.5.3 DNA cloning into a suitable vector
3.5.3.1 Fragment amplification by PCR and purification of PCR product
3.5.3.2 Ligation of amplified fragments by PCR into transient vectors
3.5.4 Transformation of the host cells
3.5.4.1 Competent cells preparation
3.5.4.2 Transformation
3.5.4.3 Preparation of plasmid DNA
3.5.4.4 Fragment restriction and ligation into expression vector
3.5.5 Induction of the expression of the desired protein under controlled conditions
3.5.6 Recovery and purification of the recombinant product
3.5.7 Preparation and encapsulation of recombinant peptides
3.6 Summary
References
4 Methodologies for extraction and separation of short-chain bioactive peptides
4.1 Introduction
4.2 Definition: Short-chain peptide enrichment
4.3 Materials, equipment and reagents
4.4 Protocols
4.5 Pros and cons
4.6 Alternative methods/procedures
4.7 Troubleshooting & Optimization
4.8 Materials, equipment and reagents
4.9 Protocols
4.10 Pros and cons
4.11 Alternative methods/procedures
4.12 Troubleshooting & Optimization
4.13 Summary
References
5 Methodologies for peptidomics: Identification and quantification
5.1 Introduction
5.2 Identification of naturally generated peptides
5.3 Materials, equipment, and reagents
5.3.1 Protocol
5.3.2 Analysis and statistics
5.3.3 Pros and cons
5.3.4 Alternative methods/procedures
5.3.5 Troubleshooting and optimization
5.4 Label-free relative quantitation of naturally generated peptides
5.4.1 Materials, equipment, and reagents
5.4.2 Protocols
5.4.3 Analysis and statistics
5.4.4 Pros and cons
5.4.5 Alternative methods/procedures
5.4.6 Troubleshooting and optimization
5.5 Absolute quantitation of naturally generated peptides
5.5.1 Materials, equipment, and reagents
5.5.2 Protocols
5.5.3 Analysis and statistics
5.5.4 Pros and cons
5.5.5 Alternative methods/procedures
5.5.6 Troubleshooting and optimization
5.6 Summary
References
6 Methodologies for bioactivity assay: biochemical study
6.1 Introduction
6.2 Antioxidant activity assays
6.2.1 Ferric-reducing antioxidant power assay
6.2.1.1 Definition
6.2.1.2 Materials, equipment, and reagents
6.2.1.3 Protocols
6.2.1.4 Analysis and statistics
6.2.1.5 Safety considerations and standards
6.2.1.6 Pros and cons
6.2.1.7 Precursor techniques and related techniques
6.2.2 Oxygen radical absorbance capacity (ORAC) assay
6.2.2.1 Definition
6.2.2.2 Materials, equipment, and reagents
6.2.2.3 Protocols
6.2.2.4 Analysis and statistics
6.2.2.5 Safety considerations and standards
6.2.2.6 Pros and cons
6.2.2.7 Precursor techniques and related techniques
6.2.3 Trolox-equivalent antioxidant capacity assay
6.2.3.1 Definition
6.2.3.2 Materials, equipment, and reagents
6.2.3.3 Protocol
6.2.3.4 Analysis and statistics
6.2.3.5 Safety considerations and standards
6.2.3.6 Pros and cons
6.2.3.7 Precursor and related techniques
6.2.4 Other antioxidant activity assays
6.3 Enzyme inhibitory assays
6.3.1 Assay of angiotensin-I-converting enzyme inhibition
6.3.1.1 Definition
6.3.1.2 Materials, equipment, and reagents
6.3.1.3 Protocol
6.3.1.4 Analysis and statistics
6.3.1.5 Alternative methods/procedures
6.3.2 Assay of renin inhibition
6.3.2.1 Definition
6.3.2.2 Materials, equipment, and reagents
6.3.2.3 Protocols
6.3.2.4 Analysis and statistics
6.3.2.5 Alternative methods/procedures
6.3.3 Assay of dipeptidyl peptidase IV inhibitory activity
6.3.3.1 Definition
6.3.3.2 Materials, equipment, and reagents
6.3.3.3 Protocols
6.3.3.4 Analysis and statistics
6.3.3.5 Precursor and related techniques
6.3.3.6 Alternative methods/procedures
6.3.4 Assay of α-amylase inhibitory activity
6.3.4.1 Definition
6.3.4.2 Materials, equipment, and reagents
6.3.4.3 Protocols
6.3.4.4 Analysis and statistics
6.3.4.5 Precursor and related techniques
6.3.4.6 Alternative methods/procedures
6.3.5 Assay of α-glucosidase inhibitory activity
6.3.5.1 Definition
6.3.5.2 Materials, equipment, and reagents
6.3.5.3 Protocols
6.3.5.4 Analysis and statistics
6.3.5.5 Precursor and related techniques
6.3.5.6 Alternative methods/procedures
6.3.6 Assay of lipase inhibitory activity
6.3.6.1 Definition
6.3.6.2 Assay A
6.3.6.2.1 Materials, equipment, and reagents
6.3.6.2.2 Protocols
6.3.6.2.3 Analysis and statistics
6.3.6.3 Assay B
6.3.6.3.1 Materials, equipment, and reagents
6.3.6.3.2 Protocols
6.3.6.3.3 Analysis and statistics
6.3.7 Assay of tyrosinase inhibitory activity
6.3.7.1 Definition
6.3.7.2 Materials, equipment, and reagents
6.3.7.3 Protocols
6.3.7.4 Analysis and statistics
6.3.7.5 Precursor and related techniques
6.3.7.6 Alternative methods/procedures
6.3.8 Assay of trypsin inhibitory activity
6.3.8.1 Definition
6.3.8.2 Materials, equipment, and reagents
6.3.8.3 Protocols
6.3.8.4 Analysis and statistics
6.3.8.5 Precursor and related techniques
6.3.8.6 Alternative methods/procedures
6.3.9 Assay of chymotrypsin inhibitory activity
6.3.9.1 Definition
6.3.9.2 Materials, equipment, and reagents
6.3.9.3 Protocols
6.3.9.4 Analysis and statistics
6.3.9.5 Precursor and related techniques
6.3.9.6 Alternative methods/procedures
6.3.10 Assay of acetylcholinesterase inhibitory activity
6.3.10.1 Definition
6.3.10.2 Materials, equipment, and reagents
6.3.10.3 Protocols
6.3.10.4 Analysis and statistics
6.3.10.5 Precursor and related techniques
6.3.10.6 Alternative methods/procedures
6.3.11 Pros and cons
6.3.12 Troubleshooting and optimization
6.4 Summary
Acknowledgments
References
7 Methodologies for bioactivity assay: cell study
7.1 Introduction
7.2 Cell culture basics
7.2.1 Basic equipment for cell culture
7.2.2 Safety aspects of cell culture
7.2.2.1 Risk assessment
7.2.2.2 Biohazards
7.2.2.3 Disinfection
7.2.2.4 Waste disposal
7.2.3 Aseptic technique and contamination control
7.2.3.1 Personal hygiene
7.2.3.2 Sterile work area—biosafety cabinet
7.2.3.3 Sterile reagent and media
7.2.4 Cell types and sourcing of cell lines
7.2.4.1 Primary cultures
7.2.4.2 Continuous cultures
7.2.4.3 Selecting the appropriate cell line
7.2.4.4 Sourcing cell lines
7.2.5 Cell culture conditions
7.2.5.1 Culture media
7.2.5.2 Temperature, pH, CO2, and O2 levels
7.2.5.3 Subculturing
7.3 Basic cell culture protocols
7.3.1 Protocol 1. Subculturing adherent cultures
7.3.2 Protocol 2. Subculturing suspension cultures
7.3.3 Protocol 3. Quantification of total cell number and cell viability
7.3.4 Protocol 4. Freezing cells
7.3.5 Protocol 5. Thawing cryopreserved cells
7.4 Study bone health-promoting peptide
7.4.1 Bone formation cells
7.4.1.1 Protocol 6. In vitro osteoblasts culturing
MC3T3-E1 cell line (ATCC CRL-2593)
Materials, equipment, and reagents
Method
7.4.1.2 Protocol 7. Mineralization assay—Alizarin Red S staining assay
Materials, equipment, and reagents
Method
7.4.2 Bone resorption cells
7.4.2.1 Protocol 8. In vitro macrophage RAW 264.7 cell culture
RAW 264.7 cell line (ATCC TIB-71)
Materials, equipment, and reagents
Method
7.4.2.2 Protocol 9. The generation of osteoclast from macrophage RAW 264.7
Materials, equipment, and reagents
Method
7.4.2.3 Protocol 10. Tartrate resistant acid phosphatase staining
Materials, equipment, and reagents
Method
7.4.2.4 Protocol 11. Osteoclastic resorption assay
Materials, equipment, and reagents
Method
7.5 Biochemical and molecular analysis of cell study
7.5.1 Protocol 12. Western blotting
7.5.1.1 Materials, equipment, and reagents
7.5.1.2 Method
7.5.1.3 Preparation of cell lysate
7.5.1.4 Preparation of SDS polyacrylamide gel [Note 10]
7.5.1.5 Electrophoresis
7.5.1.6 Electrophoretic transfer from gel to membrane
7.5.1.7 Protein detection
7.5.2 Protocol 13. Quantitative reverse transcription polymerase chain reaction
7.5.2.1 Materials, equipment, and reagents
7.5.2.2 Method
7.5.2.3 RNA extraction by TRIzol reagent [Note 2]
7.5.2.4 Reverse transcription
7.5.2.5 Design primers for SYBR Green qPCR assay
7.5.2.6 Perform quantitative reverse transcription polymerase chain reaction using SYBR Green assay
7.5.2.7 Analysis of quantitative reverse transcription polymerase chain reaction data: comparative CT methods [Note 7]
7.6 Summary
References
8 Methodologies for bioactivity assay: animal study
Abbreviations
8.1 Introduction
8.2 Administration of food peptides and animal safety
8.2.1 Safety and toxicological evaluation of peptides
8.2.2 Meal feeding information
8.2.3 Distribution of gender and age
8.2.4 Development of oral and injectable peptides derived from food
8.3 Animal models to evaluate hypertension
8.3.1 Classical animal models to evaluate hypertension
8.3.2 Newfangled animal models to evaluate hypertension and cardiovascular disease
8.4 Animal models to evaluate metabolic dysfunction
8.4.1 Animal models to evaluate metabolic dysfunction
8.4.2 Knockout mice models to evaluate metabolic dysfunction
8.5 Analysis and statistics
8.5.1 Sample size: power analysis
8.5.2 Handling of normal and nonnormal distributed data
8.5.3 Multivariate analysis of animal studies
8.6 Safety considerations and standards during the development of animal models
8.6.1 Bioethics considerations
8.6.2 Clinical evaluation of sick animals
8.7 Summary
References
9 Methodologies for bioavailability assessment of food-derived peptide
9.1 Introduction
9.2 Structure of peptides in foods
9.3 Presence of food-derived peptides with modified amino acid residues in blood
9.4 Direct identification of food-derived peptides in the body
9.5 Detection of exopeptidase-resistant peptides in blood
9.6 Peptides pass through Caco-2 monolayer
9.7 Biological activity of food-derived peptides in body
9.8 Conclusion and future prospects
References
10 Methodologies for studying the structure–function relationship of food-derived peptides with biological activities
10.1 Introduction
10.2 Bioactivity prediction of peptides
10.3 Mapping methods to predict structure–function of bioactive peptides
10.4 In silico methods predicting bioactivity in food-derived peptides
10.5 Methods to analyze the physicochemical feature of bioactive peptide
10.6 Quantitative structure–activity relationship methods to assess food-derived peptide functions
10.7 Artificial neural networking and quantitative structure–activity relationship integrative approach to assess bioactive...
10.8 Limitations of classical bioinformatics and computational biology approach for peptide analysis
10.9 Conclusion and future directions
References
11 Methodologies for investigating the vasorelaxation action of peptides
11.1 Introduction
11.2 Principles
11.2.1 Measurement of vascular tension
11.2.2 Measurement of [Ca2+]i
11.2.3 Assay for Ca2+–CaM complex formation
11.3 Materials, equipments, and reagents
11.3.1 Measurement of vascular tension
11.3.1.1 Materials
11.3.1.2 Equipment
11.3.1.3 Reagents
11.3.2 Measurement of intracellular Ca2+ concentration [Ca2+]i
11.3.2.1 Materials
11.3.2.2 Equipments
11.3.2.3 Reagents
11.3.3 Assay for Ca2+–CaM complex formation
11.3.3.1 Materials
11.3.3.2 Equipments
11.3.3.3 Reagents
11.4 Protocols
11.4.1 Measurement of vascular tension
11.4.1.1 Preparation of aortic rings from rats
11.4.1.2 Measurement of vasorelaxation tension in contracted rat aortic rings
11.4.2 Measurement of [Ca2+]i
11.4.2.1 Cell culture
11.4.2.2 Measurement of [Ca2+]i in vascular smooth muscle cells
11.4.3 Assay for Ca2+–CaM complex formation
11.5 Analysis and statistics
11.5.1 Measurement of vascular tension
11.5.2 Measurement of [Ca2+]i
11.5.3 Percentage of Ca2+–CaM complex formation
11.5.4 The Hill-plot analysis
11.6 Safety considerations and standards
11.6.1 Animal ethics
11.6.1.1 Ethical statement
11.6.1.2 Protocol for euthanasia
11.7 Pros and cons
11.7.1 Measurement of vascular tension
11.7.2 Measurement of [Ca2+]i
11.7.3 Assay for Ca2+–CaM complex formation
11.8 Alternative methods/procedures
11.8.1 Measurement of vascular tension using rat mesenteric arteries
11.8.2 The patch clamp test
11.9 Troubleshooting and optimization
11.9.1 Measurement of vascular tension
11.9.2 Measurement of [Ca2+]i
11.10 Summary
References
12 Methodologies for studying mechanisms of action of bioactive peptides: a multiomic approach
12.1 Introduction
12.2 Investigation of the regulatory properties of dietary peptides in cellular signaling events
12.2.1 In silico approach for characterizing bioactive peptides
12.2.2 In silico approach for investigation of the interaction between bioactive peptides and molecular target
12.2.3 Exploration of the molecular basis of the dietary peptide modulating cellular signaling transduction via an integrat...
12.3 Conclusion
References
13 CRISPR–Cas systems in bioactive peptide research
13.1 Introduction
13.2 Timeline and development of CRISPR–Cas system
13.3 Beyond Cas9
13.4 Advancing biological research
13.5 Bioactive peptides and CRISPR–Cas9
13.5.1 Generating CRISPR-guided targets for peptide-based studies in mammalian cells
13.6 Materials, equipment, and reagents
13.7 Protocols
13.8 Analysis and quality control
13.9 Ethical reflections
13.10 Future directions
13.11 Conclusions
References
14 Databases of bioactive peptides
14.1 Introduction
14.2 General overview of databases and their classification
14.3 Biological and chemical information on peptides in brief
14.4 Some databases of bioactive peptide sequences
14.5 Using bioinformatic databases for the analysis of food proteins and peptides
14.6 Conclusion
Acknowledgments
References
15 Encapsulation technology for protection and delivery of bioactive peptides
15.1 Introduction
15.2 Microparticulate delivery systems
15.2.1 Food-grade microparticulate carrier materials
15.2.1.1 Polysaccharide-based carriers
15.2.1.2 Protein-based carriers
15.2.1.3 Lipid-based carriers
15.2.2 Techniques for fabricating microparticles
15.2.2.1 Spray drying
15.2.2.2 Coacervation
15.2.3 Bitter taste and hygroscopicity of microencapsulated peptides
15.2.3.1 Bitter taste
15.2.3.2 Hygroscopicity
15.2.4 Release characteristics, gastric stability, and bioavailability of microencapsulated peptides
15.3 Hydrogel delivery systems
15.3.1 Fabrication of bioactive peptide-loaded microgels
15.3.1.1 Injection–gelation method
15.3.1.2 Emulsion templating
15.3.2 Encapsulation efficiency of bioactive peptides in microgels
15.3.3 Release behavior and bioactive properties of encapsulated peptides in microgels
15.4 Nanoparticulate delivery systems for bioactive peptides
15.4.1 Liposome-based nanoencapsulation system for bioactive peptides
15.4.2 Polyelectrolyte-based nanoencapsulation system for bioactive peptide delivery
15.4.3 Nanoemulsion-based delivery system for bioactive peptides delivery
15.4.4 Solid lipid nanoparticles for bioactive peptide delivery
15.5 Conclusion and future perspectives
References
16 Plant sources of bioactive peptides
16.1 Introduction
16.2 Plant proteins classification and isolation and extraction methods
16.3 Sources and production of bioactive plant peptides
16.3.1 Naturally occurring bioactive peptides in plants
16.3.2 Plant-derived bioactive peptides through enzymatic hydrolysis
16.3.3 Plant-derived bioactive peptides through fermentation
16.3.4 Unique aspects of plant proteins and preparing bioactive peptides from plant sources
16.4 Mechanistic insights on the biological activities of bioactive peptides from plants
16.4.1 The role of plant-derived peptides in inflammation and immunomodulation
16.4.2 The anticancer effect of plant-derived peptides: prevention, initiation, and progression
16.4.3 The role of plant-derived peptides in metabolic syndrome
16.5 Challenges and opportunities in studying the health benefits of plant-derived peptides
16.6 Conclusion
Acknowledgements
References
17 Generation of bioactivities from proteins of animal sources by enzymatic hydrolysis and the Maillard reaction
17.1 Introduction
17.2 Bioactive peptides from milk
17.2.1 Generation of peptides from milk
17.2.2 Utilization of cheese whey for producing peptides
17.2.3 Evaluation of milk proteins for bioactive peptides
17.3 Bioactive peptides from meat
17.3.1 Generation of peptides by gastrointestinal digestion
17.3.2 Generation of peptides during aging
17.3.3 Generation of peptides during fermentation
17.3.4 Generation of peptides by protease treatments
17.4 Bioactive peptides from animal by-products
17.4.1 Generation of peptides from blood
17.4.2 Generation of peptides from collagen
17.5 Bioactive peptides from marine sources
17.5.1 Generation of peptides from seafood and its by-products
17.5.2 Commercial development of marine-derived peptides
17.6 Bioactive peptides and the Maillard reaction
17.6.1 The Maillard reaction
17.6.2 The Maillard reaction and meat
17.6.3 Bioactivities of Maillard reaction products from peptides
17.6.4 Bioactivities of volatile Maillard reaction products from peptides
17.7 Conclusion
References
18 Sustainable, alternative sources of bioactive peptides
18.1 Introduction
18.2 Fungi
18.2.1 Major fungi protein and mechanisms of extraction
18.2.2 Bioactive properties of peptides derived from fungi
18.3 Edible insects
18.3.1 Extraction of bioactive peptides from insects
18.3.2 Bioactivity of peptides derived from insects
18.4 Marine macroalgae
18.4.1 Mechanisms of extraction of bioactive peptides from marine macroalgae
18.4.2 Bioactive properties of peptides from macroalgae proteins
18.5 Underutilized agricultural by-products
18.5.1 Mechanisms for extraction of bioactive peptides from underutilized agricultural by-products
18.5.2 Bioactivity of peptides derived from underutilized agricultural by-products
18.6 Conclusion
References
19 Application in nutrition: mineral binding
19.1 Introduction
19.2 Importance of minerals for nutrition
19.2.1 Main mineral involved in nutrition and their needs in human
19.2.2 Safety considerations and standards/regulation
19.2.3 Bioavailability and metabolism of minerals
19.3 Evidence of health effects of mineral-binding peptide
19.4 Mineral-binding peptides: potential applications, sources, production, and commercialization
19.4.1 Application of mineral-binding peptides in nutrition
19.4.1.1 In case of mineral deficiency
19.4.1.2 In case of oxidation phenomena
19.4.2 Sources of mineral-binding peptides
19.4.2.1 Mineral-binding peptide in natural resources
19.4.2.2 Production of mineral-binding peptide
19.4.2.2.1 Proteolysis
19.4.2.2.2 Chemical peptide synthesis
19.5 Selective extraction of mineral-binding peptides from complex hydrolyzates
19.5.1 Peptides–metal ion interactions
19.5.2 Mineral-binding peptide screening techniques
19.5.2.1 Spectroscopic techniques
19.5.2.1.1 Principle of spectroscopic techniques
19.5.2.1.2 Use of spectroscopic techniques to understand metal–peptide interactions
19.5.2.2 Isothermal titration calorimetry
19.5.2.2.1 Principle of isothermal titration calorimetry
19.5.2.2.2 Use of ITC for MBP screening
19.5.2.3 Surface plasmon resonance
19.5.2.3.1 Principle of surface plasmon resonance
19.5.2.3.2 Use of SPR for MBP screening
19.5.2.4 Electrically switchable nanolever technology
19.5.2.4.1 Principle of the switchSENSE technology
19.5.2.4.2 Application of switchSENSE for mineral-binding peptide screening
19.5.2.5 Electrospray ionization-mass spectrometry
19.5.2.5.1 Principle of electrospray ionization-mass spectrometry
19.5.2.5.2 Use of ESI-MS for MBP screening
19.5.3 Immobilized metal-ion affinity chromatography separation
19.5.3.1 Principle of immobilized metal-ion affinity chromatography
19.5.3.2 Use of IMAC for MBP screening
19.6 Summary
Acknowledgment
References
20 Applications in nutrition: clinical nutrition
20.1 Introduction
20.1.1 Overview of clinical nutritional support and clinical nutrition therapy
20.1.2 Application of biologically active peptides in clinical nutritional support and therapy
20.2 Application of biologically active peptides in disease treatment
20.2.1 Application of biologically active peptides in the clinical treatment of cardiovascular diseases
20.2.2 Application of biologically active peptides in the clinical treatment of cancer
20.2.3 Application of biologically active peptides in the clinical treatment of liver injury
20.2.4 Application of biologically active peptides in the clinical treatment of diabetes mellitus
20.2.5 Application of biologically active peptides in the clinical treatment of other diseases
20.3 Application of biologically active peptides in clinical nutritional foods
20.3.1 Determination of proportions of biologically active peptides in products with specific nutritional requirements
20.3.1.1 Characteristics of clinical nitrogen supplementation products
20.3.1.2 Nitrogen intake requirements for different patients
20.3.1.3 Design requirements for clinical biologically active peptide products
20.3.2 Source selection of biologically active peptides in products for patients with specific health needs
20.3.3 Product forms
20.4 Summary and prospects
References
21 Applications in nutrition: sport nutrition
21.1 Introduction
21.2 Rationale
21.3 Application in sports nutrition
21.3.1 Bioactive peptides, body composition, and muscular performance
21.3.2 Bioactive peptides and muscle damage
21.3.2.1 Mechanisms
21.3.2.1.1 Effects on protein synthesis
21.3.2.1.2 Antiinflammatory effect
21.3.2.1.3 Antioxidant activity
21.3.2.2 Interim conclusion
21.3.3 Bioactive peptides and connective tissue
21.3.3.1 Tendon
21.3.3.2 Cartilage and functional joint pain
21.3.3.3 Interim conclusion
21.4 Limitations
21.5 Practical applications
21.6 Summary
References
22 Application in nutrition: cholesterol-lowering activity
22.1 Introduction
22.2 Rationale: peptides activity and characterization
22.3 Peptides from plant proteins
22.3.1 Soybean peptides
22.3.2 Lupin peptides
22.3.3 Hempseed peptides
22.4 Hypocholesterolemic peptide from other seeds: amaranth, cowpea, and rice
22.5 Peptides from animal sources
22.5.1 Milk peptides
22.5.2 Meat peptides
22.5.3 Fish peptides
22.5.4 Egg peptides
22.5.5 Royal jelly peptides
22.6 Structure–activity relationship of hypocholesterolemic peptides
22.7 Summary
References
23 Applications in nutrition: Peptides as taste enhancers
23.1 Introduction
23.2 Umami and umami-enhancing peptides
23.2.1 Umami taste
23.2.2 Umami taste receptors
23.2.3 Structural characteristics of umami and umami-enhancing peptides
23.3 Bitter and bitter inhibitory peptides
23.3.1 Bitter taste
23.3.2 Bitter taste receptor
23.3.3 Bitter taste inhibitory peptides
23.4 Salt taste-enhancing peptides
23.4.1 Salt taste
23.4.2 Salty taste receptors
23.4.3 Structural characteristics of salty taste-enhancing peptides
23.5 Kokumi peptides
23.5.1 Kokumi taste
23.5.2 Kokumi taste receptors
23.5.3 The characteristics of kokumi peptides
23.6 Summary
Acknowledgments
References
24 Cardiovascular benefits of food protein-derived bioactive peptides
24.1 Introduction
24.2 Inhibition of the renin–angiotensin–aldosterone system: antihypertensive peptides
24.2.1 ACE- and renin-inhibitory peptides
24.2.1.1 Animal protein-derived hydrolysates and peptides
24.2.1.2 Plant protein-derived hydrolysates and peptides
24.2.2 Foods formulated with antihypertensive protein hydrolysates and peptides
24.3 Conclusions
24.4 Future trends
References
25 Applications in medicine: hypoglycemic peptides
25.1 Introduction
25.2 Carbohydrate digestion and glucose homeostasis
25.3 Pathophysiology of type 2 diabetes
25.4 Clinical diagnosis of diabetes
25.5 Diverse physiological properties of protein hydrolysates and bioactive peptides
25.6 Antidiabetic properties of protein hydrolysates/peptides (in vivo studies)
25.7 Antidiabetic properties of protein hydrolysates/peptides (clinical studies)
25.8 Conclusions
References
26 Application in medicine: obesity and satiety control
Abbreviations
26.1 Introduction
26.2 Synthetic peptides
26.2.1 Synthetic peptides: glucagon-like peptide-1 mimetics
26.2.2 Synthetic peptides: multiple actions mimetics
26.2.3 Safety considerations and limitations for synthetic peptides
26.2.4 Other synthetic peptides in preclinical trials and in vitro development
26.3 Food-derived peptides
26.3.1 Food-derived peptides targeting CCK and GI enzymes with proven in vivo efficacy
26.3.2 Food-derived peptides targeting ghrelin, opioid receptor, and GI transit with proven in vivo efficacy
26.3.3 Food-derived peptides targeting lipid metabolism with proven in vivo efficacy
26.3.4 Food-derived peptides inhibiting protease dipeptidyl peptidase-4
26.3.5 In vitro evidence of food-derived peptides
26.3.6 Limitations: survival of food-derived peptides during gut transit
26.4 Commercial dietary protein hydrolyzates with antiobesity potential
26.5 Summary
Acknowledgments
References
27 Food-derived osteogenic peptides towards osteoporosis
27.1 Introduction
27.2 Evaluation and diagnosis of osteoporosis
27.2.1 Bone formation and resorption biomarkers
27.2.2 Computed tomography diagnosis
27.3 Osteogenic agents
27.3.1 Drugs for osteoporosis
27.3.2 Osteogenic peptides
27.4 Characterization of osteogenic peptides
27.4.1 Preparation of osteogenic peptides
27.4.2 Identification of osteogenic peptides
27.5 Bioavailability of osteogenic peptides
27.5.1 Absorption analysis
27.5.2 Pharmacokinetic analysis
27.6 Conclusions
Acknowledgments
Reference
28 Applications in medicine: mental health
28.1 Introduction
28.1.1 Peptide transport across the blood–brain barrier and use as shuttles
28.2 Peptides as diagnostic tools in brain tumors and CNS disorders
28.2.1 Peptide-based imaging tracers
28.2.2 Peptides as biomarkers
28.3 Therapeutic applications of peptides for mental health
28.3.1 Neurodevelopmental disorders
28.3.2 Psychotic disorders
28.3.3 Depressive, bipolar, and anxiety disorders
28.3.4 Neurocognitive and neurodegenerative disorders
28.3.5 Others
28.4 Conclusion
References
29 Applications in medicine: joint health
29.1 Introduction
29.2 Overview of joint diseases
29.2.1 Osteoarthritis
29.2.2 Rheumatoid arthritis
29.3 Peptides activity and characterization
29.3.1 Natural bioactive peptide sources
29.3.2 Peptidome analysis
29.4 Mechanisms of action
29.4.1 Cartilage proliferation
29.4.2 Antioxidant, antimicrobial, and antiinflammatory activities
29.4.3 Neuroactivity
29.5 Evidence in joint health benefits
29.6 Potential applications, production, and commercialization
29.6.1 Diagnostic
29.6.2 Prophylaxis/therapeutic
29.6.3 Production and commercialization
29.7 Summary
Acknowledgments
References
30 Applications in food technology: antimicrobial peptides
30.1 Introduction
30.2 Classification
30.3 Current and potential food applications
30.3.1 Commercial application of nisin
30.3.2 Commercial application of pediocin
30.3.3 Commercial application of MicroGARD
30.3.4 Commercial application of ε-polylysine
30.3.5 Other antimicrobial peptide preparations received regulatory approval
30.4 Hurdle approach
30.5 Application of antimicrobial peptides for improving human health
30.5.1 Antimicrobial peptides production by probiotic strains
30.5.2 Antiinfective activity of antimicrobial peptides
30.5.3 Antiviral effect of antimicrobial peptides
30.5.4 Bioavailability and metabolism
30.6 Mechanisms of action
30.6.1 Mechanisms of action against bacteria and fungi
30.6.2 Mechanisms of action against viruses
30.7 Safety considerations and regulations
30.7.1 Safety of antimicrobial peptides
30.7.2 Regulatory aspects of using AMPs or AMP producers in food
30.8 Limitations
30.9 Summary
References
Index
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