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Arthropod Venom Components and Their Potential Usage

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ISBN: 9783039285402 9783039285419 Year: Pages: 404 DOI: 10.3390/books978-3-03928-541-9 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Public Health --- Medicine (General)
Added to DOAB on : 2020-04-07 23:07:09
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Abstract

Thousands of arthropod species, ranging from arachnids (spiders and scorpions) to hymenopterans (ants, bees, and wasps) and myriapods (centipedes), are venomous and use their venoms for both defense and predation. These venoms are invariably harmful to humans, and some may cause serious injuries, e.g., those from scorpions, spiders, and wasps. Arthropods’ venoms are also known as rich sources of biologically active compounds and have attracted the attention of toxin researchers for years. In this century, venom component analysis has progressed considerable due to the advances in analytical techniques, in particular, mass spectrometry and next-generation deep (DNA and RNA) sequencing. As such, proteomic and peptidomic analyses using LC–MS have enabled the full analysis of venom components, revealing a variety of novel peptide and protein toxins sequences and scaffolds, potentially useful as pharmacological research tools and for the development of highly selective peptide ligands and therapeutic leads, like chlorotoxin. Due to their specificity for numerous ion-channel subtypes, including voltage- and ligand-gated ion channels, arthropod neurotoxins have been investigated to dissect and treat neurodegenerative diseases and control epileptic syndromes. This Special Issue collects information on such progress, encouraging contributions on the chemical and biological characterization of venom components, not only peptides and proteins, but also small molecules, their mechanisms of action, and the development of venom-derived peptide leads.

Keywords

ant --- venom --- mass spectrometry analysis --- pilosulin-like peptide --- phospholipases D --- metalloproteases --- Loxosceles spp. --- recombinant toxins --- hybrid immunogen --- neutralizing antibodies --- antivenoms --- LyeTxI-b --- Staphylococcus aureus --- keratitis --- AMP --- mastoparan --- Acinetobacter baumannii --- stent --- cantharidin --- blister beetle --- Berberomeloe majalis --- nematicide --- ixodicide --- antifeedant --- scorpion venom --- insecticidal peptide --- mass spectrometric analysis --- de novo sequencing --- Centruroides limpidus Karch --- proteome --- scorpion --- transcriptome --- venom toxicity --- brown spider --- venom --- Loxosceles --- toxins --- biotools --- drug targets --- novel therapeutics --- spider toxin --- directed disulfide bond formation --- Nav channel activity --- Nav1.7 --- pain target --- automated patch-clamp --- bee venom --- alternative treatment --- skin --- cutaneous disease --- mechanism --- chemotherapy --- cold allodynia --- mechanical allodynia --- melittin --- neuropathic pain --- oxaliplatin --- natural antibiotics --- piperidine heterocyclic amines --- industrial biotechnology --- LTQ Orbitrap Hybrid Mass Spectrometer --- myrmecology --- venom --- pain --- ants --- wasps --- bees --- Hymenoptera --- envenomation --- toxins --- peptides --- pharmacology --- Dinoponera quadriceps --- Formicidae --- Hymenoptera venom --- proteomics --- venom allergens --- ICK-like toxins --- melittin --- insect immune system --- apoptosis --- heart contractility --- Tenebrio molitor --- bee venom --- bioinformatics --- computational docking --- homology modelling --- ion channel structure --- protein–peptide interactions --- tertiapin --- venom peptides --- virtual screening --- small hive beetle --- solitary wasp --- venom --- antimicrobial peptide --- linear cationic ?-helical peptide --- amphipathic ?-helix structure --- channel-like pore-forming activity --- antimicrobial peptide --- venom --- arthropod --- malaria --- Chagas disease --- human African trypanosomiasis --- leishmaniasis --- toxoplasmosis --- venom peptides --- FMRF-amide --- insect neurotoxin --- protons --- pH regulation --- acid-sensing ion channels --- acid-gated currents --- chronic pain --- ICK peptide --- knottins --- NaV --- spider venom --- voltage-gated sodium channel --- n/a

Toxins in Drug Discovery and Pharmacology

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ISBN: 9783038428619 9783038428626 Year: Pages: XII, 304 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Public Health
Added to DOAB on : 2018-05-04 11:37:49
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Venoms from marine and terrestrial animals (cone snails, scorpions, spiders, snakes, centipedes, cnidarian, etc.) can be seen as untapped cocktails of biologically active compounds that are being increasingly recognized as a new emerging source of peptide-based therapeutics. Venomous animals are considered to be specialized predators that have evolved the most sophisticated peptide chemistry and neuropharmacology for their own biological purposes by producing venoms that contain a structural and functional diversity of neurotoxins. These neurotoxins appear to be highly selective ligands for a wide range of ion channels and receptors. Therefore, they represent interesting lead compounds for the development of analgesics, anti-cancer drugs, drugs for neurological disorders such as multiple sclerosis, Parkinson' s disease, Alzheimer' s disease, and other therapeutics.This Special Issue of Toxins aims to provide a comprehensive look at toxins and toxin-inspired leads and will focus on the mechanisms of action, structure–function relationships, and evolution of pharmacologically interesting venom components, including the most recent developments related to the emergence of venoms as an underutilized source of highly evolved bioactive peptides with clinical potential.

Venom and Toxin as Targeted Therapy

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ISBN: 9783039211890 9783039211906 Year: Pages: 180 DOI: 10.3390/books978-3-03921-190-6 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology
Added to DOAB on : 2019-12-09 11:49:15
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Targeted therapy has developed significantly in the last one and half decades, prescribing specific medications for treatment of particular diseases, such as cancer, diabetes, and heart disease. One of the most exciting recent developments in targeted therapies was the isolation of disease-specific molecules from natural resources, such as animal venoms and plant metabolites/toxins, for use as templates for new drug motif designs. In addition, the study of venom proteins/peptides and toxins naturally targeted mammalian receptors and demonstrated high specificity and selectivity towards defined ion channels of cell membranes. Research has also focsed intensely on receptors. The focus of this Special Issue of Toxins addressed the most recent advances using animal venoms, such as frog secretions, bee/ant venoms and plant/fungi toxins, as medicinal therapy. Recent advances in venom/toxin/immunotoxins for targeted cancer therapy and immunotherapy, along with using novel disease-specific venom-based protein/peptide/toxin and currently available FDA-approved drugs for combinationtreatments will be discussed. Finally, we included an overview of select promising toad/snake venom-based peptides/toxins potentially able to address the forthcoming challenges in this field. Both research and review articles proposing novelties or overviews, respectively, were published in this Special Issue after rigorous evaluation and revision by expert peer reviewers.

Keywords

disintegrin --- blood vessel formation --- VEGF --- antioxidant enzymes --- oxidative stress biomarkers --- bicarinalin --- antimicrobial peptide --- Helicobacter pylori --- gastric cells --- bacterial adhesion --- SEM --- atopic dermatitis (AD) --- house dust mite extract (DFE) --- 2,4-dinitrochlorobenzene (DNCB) --- bee venom phospholipase A2 (bvPLA2) --- skin inflammation --- CD206 --- mannose receptor --- immunotoxin --- Moxetumomab pasudotox --- targeted therapy --- CD22 --- B cell non-Hodgkin lymphoma --- acute lymphoblastic leukemia --- mantle cell lymphoma --- ribosome-inactivating protein --- BLF1 --- eIF4A --- MYCN --- cancer --- neuroblastoma --- apoptosis --- antimicrobial peptide (AMP) --- dermaseptin --- anuran skin secretion --- drug design --- antimicrobial activity --- anticancer activity --- antiviral activity --- Bougainvillea --- bouganin --- cancer therapy --- immunotherapy --- immunotoxins --- ribosome-inactivating proteins --- rRNA N-glycosylase activity --- VB6-845 --- orellanine --- clearance --- fungal toxin --- half-life --- toad toxins --- Chansu --- Huachansu --- cane toad --- bufadienolides --- indolealkylamines --- inflammation --- cancer --- obsessive–compulsive disorder (OCD) --- snake venom --- cancer --- target therapy --- snake venom --- Malaysian cobras --- N. kaouthia --- N. sumatrana --- O. hannah --- anticancer --- Apis mellifera syriaca --- bee venom --- melittin --- LC-ESI-MS --- solid phase extraction --- in vitro effects --- frog --- mass spectrometry --- molecular cloning --- bombesin-related peptide --- smooth muscle --- Bee venom --- complement system --- decay accelerating factor --- atopic dermatitis --- complement dependent cytotoxicity --- membrane attack complex --- n/a

Analysis of Peptides and Proteins by Electrophoretic Techniques

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ISBN: 9783039212279 9783039212286 Year: Pages: 110 DOI: 10.3390/books978-3-03921-228-6 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Chemistry (General)
Added to DOAB on : 2019-08-28 11:21:27
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The characterization of peptides and proteins is central to understanding their function and expression in biological matrices. Moreover, these macromolecules are important biomarkers of many human diseases. In recent years, the performance of separation techniques based on electromigration have significantly increased. The development of microdevices has reduced sample consumption and waste production while high-sensitivity detectors, such as mass spectrometry (MS) or laser-induced fluorescence (LIF), have significantly improved with regards to separation efficiency and detection limits. All of these advancements have led to appreciably enlarged fields of application. Nowadays, a multitude of studies using separation techniques based on electromigration to study proteins and peptides from numerous real matrices are available in the literature. This Special Issue covers the most recent knowledge and advances in the study of peptides and proteins using several electrophoresis techniques, as well as the characterization of relevant proteins and peptides in application areas such as clinical studies, functional foods, and toxicology.

Marine Bioactive Peptides: Structure, Function, and Therapeutic Potential

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ISBN: 9783039215324 9783039215331 Year: Pages: 442 DOI: 10.3390/books978-3-03921-533-1 Language: English
Publisher: MDPI - Multidisciplinary Digital Publishing Institute
Subject: Science (General) --- Biology
Added to DOAB on : 2019-12-09 11:49:16
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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.

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 --- ?-helix --- Rana-box --- nuclear magnetic resonance (NMR) --- antimicrobial peptide --- cytotoxicity --- ?-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-1? --- 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-?B --- Nrf2 --- endothelial dysfunction --- conotoxin --- cone snail --- Conus --- Conus ateralbus --- Kalloconus --- n/a

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