Reprint
Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential
Edited by
October 2019
442 pages
- ISBN978-3-03921-532-4 (Paperback)
- ISBN978-3-03921-533-1 (PDF)
This book is a reprint of the Special Issue Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential that was published in
Biology & Life Sciences
Chemistry & Materials Science
Medicine & Pharmacology
Summary
This Special Issue Book, “Marine Bioactive Peptides: Structure, Function, andTherapeutic Potential" includes up-to-date information regarding bioactivepeptides isolated from marine organisms. Marine peptides have been found invarious phyla, and their numbers have grown in recent years. These peptidesare diverse in structure and possess broad-spectrum activities that have greatpotential for medical applications. Various marine peptides are evolutionaryancient molecular factors of innate immunity that play a key role in host defense.A plethora of biological activities, including antibacterial, antifungal, antiviral,anticancer, anticoagulant, endotoxin-binding, immune-modulating, etc., makemarine peptides an attractive molecular basis for drug design. This Special IssueBook presents new results in the isolation, structural elucidation, functionalcharacterization, and therapeutic potential evaluation of peptides found inmarine organisms. Chemical synthesis and biotechnological production of marinepeptides and their mimetics is also a focus of this Special Issue Book.
Format
- Paperback
License
© 2019 by the authors; CC BY-NC-ND license
Keywords
sea cucumber; ACE-inhibitory peptide; molecular docking; structure-activity relationship; plastein reaction; Gracilariopsis lemaneiformis; ACE-inhibitory activity; peptide; molecular docking; SHRs; prostate cancer; Anthopleura anjunae oligopeptide; DU-145 cells; PI3K/AKT/mTOR signaling pathway; cod skin; NA-inhibitory peptide; influenza virus; neuraminidase; molecular docking; adsorption; host defense peptide; antimicrobial peptide; anti-LPS factor; host‒microbe relationship; functional diversity; invertebrate immunity; crustacean; antimicrobial activity; antimicrobial peptide; polychaeta; innate immunity; BRICHOS domain; recombinant peptide; α-helix; Rana-box; nuclear magnetic resonance (NMR); antimicrobial peptide; cytotoxicity; β-hairpin; polyphemusins; tachyplesins; cell death; signaling pathways; Neptunea arthritica cumingii; multi-functional peptides; antioxidant activity; ACE-inhibitory activity; anti-diabetic activity; Arenicola marina; antimicrobial peptides; arenicin; complement; C3a; acid-sensing ion channel; animal models; pain relief; toxin; Ugr 9-1; APETx2; hairtail (Trichiurus japonicas); muscle; peptide; antioxidant activity; half-fin anchovy hydrolysates; Maillard reaction products; antibacterial peptide; identification; self-production of hydrogen peroxide; membrane damage; Perinereis aibuhitensis; decapeptide; lung cancer; cell proliferation; apoptosis; conotoxins; conopeptides; computational studies; molecular dynamics; machine learning; docking; review; drug design; ion channels; Conus; conotoxin; transcriptome sequencing; phylogeny; venom duct; abalone; peptide; vasculogenic mimicry; metastasis; MMPs; HIF-1α; dexamethasone; myotube atrophy; protein synthesis; proteolytic system; Pyropia yezoensis peptide; PYP15; QAGLSPVR; antihypertensive effect; Caco-2 cell monolayer; transport routes; oyster zinc-binding peptide; peptide-zinc complex; caco-2 cells; intestinal absorption; zinc bioavailability; Chlorella pyrenoidosa protein hydrolysate (CPPH); Chlorella pyrenoidosa protein hydrolysate-calcium chelate (CPPH-Ca); calcium absorption; gene expression; gut microbiota; cone snails; conotoxins; ion channels; function; structure; marine peptides; arenicin-1; molecular symmetry; structure–activity relationship; antibacterial; cytotoxic; chemical synthesis; molecular dynamics; tilapia; HUVEC; angiotensin II; NF-κB; Nrf2; endothelial dysfunction; conotoxin; cone snail; Conus; Conus ateralbus; Kalloconus; n/a