http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
from basic science to applications for human health
Biologically Active Peptides: From Basic Science to Applications for Human Health stands as a comprehensive resource on bioactive peptide science and applications.With contributions from more than thirty global experts, topics discussed include bioactive peptide science, structure-activity relationships, best practices for their study and.
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 &amp -- Optimization -- 4.8 Materials, equipment and reagents -- 4.9 Protocols -- 4.10 Pros and cons -- 4.11 Alternative methods/procedures -- 4.12 Troubleshooting &amp -- 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.
6.3.9 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).