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https://www.readbyqxmd.com/read/28416444/the-pharmacology-of-voltage-gated-sodium-channel-activators
#1
REVIEW
Jennifer R Deuis, Alexander Mueller, Mathilde R Israel, Irina Vetter
Toxins and venom components that target voltage-gated sodium (NaV) channels have evolved numerous times due to the importance of this class of ion channels in the normal physiological function of peripheral and central neurons as well as cardiac and skeletal muscle. NaV channel activators in particular have been isolated from the venom of spiders, wasps, snakes, scorpions, cone snails and sea anemone and are also produced by plants, bacteria and algae. These compounds have provided key insight into the molecular structure, function and pathophysiological roles of NaV channels and are important tools due to their at times exquisite subtype-selectivity...
April 14, 2017: Neuropharmacology
https://www.readbyqxmd.com/read/28411930/marine-envenomation
#2
REVIEW
Kirsten B Hornbeak, Paul S Auerbach
Venomous aquatic animals are hazardous to swimmers, surfers, divers, and fishermen. Exposures include mild stings, bites, abrasions, and lacerations. Severe envenomations can be life threatening. This article reviews common marine envenomations, exploring causative species, clinical presentation, and current treatment recommendations. Recommendations are included for cnidaria, sponges, bristle worms, crown-of-thorns starfish, sea urchins, venomous fish, stingrays, cone snails, stonefish, blue-ringed octopus, and sea snakes...
May 2017: Emergency Medicine Clinics of North America
https://www.readbyqxmd.com/read/28400262/identification-of-short-single-disulfide-containing-contryphans-from-the-venom-of-cone-snails-using-de-novo-mass-spectrometry-based-sequencing-methods
#3
Jayaseelan Benjamin Franklin, Rajaian Pushpabai Rajesh, Nambali Valsalan Vinithkumar, Ramalingam Kirubagaran
We identified 12 short single disulfide-containing conopeptides from the venom of Conus coronatus, C. leopardus, C. lividus and C. zonatus. Interestingly, we detected the shortest contryphan sequence thus far characterized which contains only six amino acid residues. We also identified three distinct contryphan sequences of C. lividus without any proline residues and one sequence with an unusual post-translational modification (bromination of tryptophan). Furthermore, we characterized venom peptides of C...
June 15, 2017: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/28398099/enhancing-the-therapeutic-potential-of-peptide-toxins
#4
Raymond S Norton
Peptide toxins are potent and often exquisitely selective probes of the structure and function of ion channels and receptors, and as such are of significant interest to the pharmaceutical and biotech industries as both therapeutic leads and pharmacological tools. Their progression as clinical candidates, however, faces many of the challenges that are common to peptide drugs generally. Areas covered: The attributes of peptide toxins as therapeutic leads are outlined, as well as some of the limiting factors that have hampered the clinical development of many promising candidates...
April 20, 2017: Expert Opinion on Drug Discovery
https://www.readbyqxmd.com/read/28396446/identification-of-a-cono-rfamide-from-the-venom-of-conus-textile-that-targets-asic3-and-enhances-muscle-pain
#5
Catharina Reimers, Cheng-Han Lee, Hubert Kalbacher, Yuemin Tian, Chih-Hsien Hung, Axel Schmidt, Lea Prokop, Silke Kauferstein, Dietrich Mebs, Chih-Cheng Chen, Stefan Gründer
Acid-sensing ion channels (ASICs) are proton-gated Na(+) channels that are expressed throughout the nervous system. ASICs have been implicated in several neuronal disorders, like ischemic stroke, neuronal inflammation, and pathological pain. Several toxins from venomous animals have been identified that target ASICs with high specificity and potency. These toxins are extremely useful in providing protein pharmacophores and to characterize function and structure of ASICs. Marine cone snails contain a high diversity of toxins in their venom such as conotoxins, which are short polypeptides stabilized by disulfide bonds, and conopeptides, which have no or only one disulfide bond...
April 10, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28238803/discovery-and-characterization-of-eiib-a-new-%C3%AE-conotoxin-from-conus-ermineus-venom-by-nachrs-affinity-capture-monitored-by-maldi-tof-tof-mass-spectrometry
#6
Julien Echterbille, Nicolas Gilles, Romulo Araóz, Gilles Mourier, Muriel Amar, Denis Servent, Edwin De Pauw, Loic Quinton
Animal toxins are peptides that often bind with remarkable affinity and selectivity to membrane receptors such as nicotinic acetylcholine receptors (nAChRs). The latter are, for example, targeted by α-conotoxins, a family of peptide toxins produced by venomous cone snails. nAChRs are implicated in numerous physiological processes explaining why the design of new pharmacological tools and the discovery of potential innovative drugs targeting these receptor channels appear so important. This work describes a methodology developed to discover new ligands of nAChRs from complex mixtures of peptides...
February 24, 2017: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/28216409/structure-and-activity-of-contryphan-vc2-importance-of-the-d-amino-acid-residue
#7
Stephen B Drane, Samuel D Robinson, Christopher A MacRaild, Sandeep Chhabra, Balasubramanyam Chittoor, Rodrigo A V Morales, Eleanor W W Leung, Alessia Belgi, Samuel S Espino, Baldomero M Olivera, Andrea J Robinson, David K Chalmers, Raymond S Norton
In natural proteins and peptides, amino acids exist almost invariably as l-isomers. There are, however, several examples of naturally-occurring peptides containing d-amino acids. In this study we investigated the role of a naturally-occurring d-amino acid in a small peptide identified in the transcriptome of a marine cone snail. This peptide belongs to a family of peptides known as contryphans, all of which contain a single d-amino acid residue. The solution structure of this peptide was solved by NMR, but further investigations with molecular dynamics simulations suggest that its solution behaviour may be more dynamic than suggested by the NMR ensemble...
February 17, 2017: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/28152596/contryphan-genes-and-mature-peptides-in-the-venom-of-nine-cone-snail-species-by-transcriptomic-and-mass-spectrometric-analysis
#8
Marimuthu Vijayasarathy, Soorej M Basheer, Jayaseelan Benjamin Franklin, Padmanabhan Balaram
The occurrence of contryphans, a class of single-disulfide-bond-containing peptides, is demonstrated by the analysis of the venom of nine species of cone snails. Ten full gene sequences and two partial gene sequences coding for contryphan precursor proteins have been identified by next-generation sequencing and compared with available sequences. The occurrence of mature peptides in isolated venom has been demonstrated by LC-ESI-MS/MS analysis. De novo sequencing of reduced, alkylated contryphans from C. frigidus and C...
February 3, 2017: Journal of Proteome Research
https://www.readbyqxmd.com/read/28148828/ocean-acidification-alters-predator-behaviour-and-reduces-predation-rate
#9
Sue-Ann Watson, Jennifer B Fields, Philip L Munday
Ocean acidification poses a range of threats to marine invertebrates; however, the emerging and likely widespread effects of rising carbon dioxide (CO2) levels on marine invertebrate behaviour are still little understood. Here, we show that ocean acidification alters and impairs key ecological behaviours of the predatory cone snail Conus marmoreus Projected near-future seawater CO2 levels (975 µatm) increased activity in this coral reef molluscivore more than threefold (from less than 4 to more than 12 mm min(-1)) and decreased the time spent buried to less than one-third when compared with the present-day control conditions (390 µatm)...
February 2017: Biology Letters
https://www.readbyqxmd.com/read/27941639/evolution-of-the-cytolytic-pore-forming-proteins-actinoporins-in-sea-anemones
#10
Jason Macrander, Marymegan Daly
Sea anemones (Cnidaria, Anthozoa, and Actiniaria) use toxic peptides to incapacitate and immobilize prey and to deter potential predators. Their toxin arsenal is complex, targeting a variety of functionally important protein complexes and macromolecules involved in cellular homeostasis. Among these, actinoporins are one of the better characterized toxins; these venom proteins form a pore in cellular membranes containing sphingomyelin. We used a combined bioinformatic and phylogenetic approach to investigate how actinoporins have evolved across three superfamilies of sea anemones (Actinioidea, Metridioidea, and Actinostoloidea)...
December 8, 2016: Toxins
https://www.readbyqxmd.com/read/27916464/subtype-specific-block-of-voltage-gated-k-channels-by-%C3%AE-conopeptides
#11
Enrico Leipold, Florian Ullrich, Markus Thiele, Alesia A Tietze, Heinrich Terlau, Diana Imhof, Stefan H Heinemann
The neurotoxic cone snail peptide μ-GIIIA specifically blocks skeletal muscle voltage-gated sodium (NaV1.4) channels. The related conopeptides μ-PIIIA and μ-SIIIA, however, exhibit a wider activity spectrum by also inhibiting the neuronal NaV channels NaV1.2 and NaV1.7. Here we demonstrate that those μ-conopeptides with a broader target range also antagonize select subtypes of voltage-gated potassium channels of the KV1 family: μ-PIIIA and μ-SIIIA inhibited KV1.1 and KV1.6 channels in the nanomolar range, while being inactive on subtypes KV1...
January 22, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27826319/in-the-picture-disulfide-poor-conopeptides-a-class-of-pharmacologically-interesting-compounds
#12
REVIEW
Eline K M Lebbe, Jan Tytgat
During evolution, nature has embraced different strategies for species to survive. One strategy, applied by predators as diverse as snakes, scorpions, sea anemones and cone snails, is using venom to immobilize or kill a prey. This venom offers a unique and extensive source of chemical diversity as it is driven by the evolutionary pressure to improve prey capture and/or to protect their species. Cone snail venom is an example of the remarkable diversity in pharmacologically active small peptides that venoms can consist of...
2016: Journal of Venomous Animals and Toxins Including Tropical Diseases
https://www.readbyqxmd.com/read/27801785/novel-conopeptides-of-largely-unexplored-indo-pacific-conus-sp
#13
Eline K M Lebbe, Maarten G K Ghequire, Steve Peigneur, Bea G Mille, Prabha Devi, Samuthirapandian Ravichandran, Etienne Waelkens, Lisette D'Souza, René De Mot, Jan Tytgat
Cone snails are predatory creatures using venom as a weapon for prey capture and defense. Since this venom is neurotoxic, the venom gland is considered as an enormous collection of pharmacologically interesting compounds having a broad spectrum of targets. As such, cone snail peptides represent an interesting treasure for drug development. Here, we report five novel peptides isolated from the venom of Conus longurionis, Conus asiaticus and Conus australis. Lo6/7a and Lo6/7b were retrieved from C. longurionis and have a cysteine framework VI/VII...
October 27, 2016: Marine Drugs
https://www.readbyqxmd.com/read/27794464/beyond-conus-phylogenetic-relationships-of-conidae-based-on-complete-mitochondrial-genomes
#14
Juan E Uribe, Nicolas Puillandre, Rafael Zardoya
Understanding how the extraordinary taxonomic and ecological diversity of cone snails (Caenogastropoda: Conidae) evolved requires a statistically robust phylogenetic framework, which thus far is not available. While recent molecular phylogenies have been able to distinguish several deep lineages within the family Conidae, including the genera Profundiconus, Californiconus, Conasprella, and Conus (and within this one, several subgenera), phylogenetic relationships among these genera remain elusive. Moreover, the possibility that additional deep lineages may exist within the family is open...
October 27, 2016: Molecular Phylogenetics and Evolution
https://www.readbyqxmd.com/read/27763551/the-snake-with-the-scorpion-s-sting-novel-three-finger-toxin-sodium-channel-activators-from-the-venom-of-the-long-glanded-blue-coral-snake-calliophis-bivirgatus
#15
Daryl C Yang, Jennifer R Deuis, Daniel Dashevsky, James Dobson, Timothy N W Jackson, Andreas Brust, Bing Xie, Ivan Koludarov, Jordan Debono, Iwan Hendrikx, Wayne C Hodgson, Peter Josh, Amanda Nouwens, Gregory J Baillie, Timothy J C Bruxner, Paul F Alewood, Kelvin Kok Peng Lim, Nathaniel Frank, Irina Vetter, Bryan G Fry
Millions of years of evolution have fine-tuned the ability of venom peptides to rapidly incapacitate both prey and potential predators. Toxicofera reptiles are characterized by serous-secreting mandibular or maxillary glands with heightened levels of protein expression. These glands are the core anatomical components of the toxicoferan venom system, which exists in myriad points along an evolutionary continuum. Neofunctionalisation of toxins is facilitated by positive selection at functional hotspots on the ancestral protein and venom proteins have undergone dynamic diversification in helodermatid and varanid lizards as well as advanced snakes...
October 18, 2016: Toxins
https://www.readbyqxmd.com/read/27712893/two-years-in-igf-research
#16
REVIEW
Briony E Forbes
The last two years of insulin-like growth factor (IGF) research has yielded a vast literature highlighting the central role IGFs factors play in processes such as development, growth, aging and neurological function. It also provides our latest understanding of how IGF system perturbation is linked to diseases including growth deficiency, cancer, and neurological and cardiovascular diseases. A snapshot of the highlights is presented in this review, focussing on the topics of IGFs and growth, comparative and structural biology to understand insulin-like peptide function, IGFs and cancer, and IGFs and neurological function...
October 2016: Growth Hormone & IGF Research
https://www.readbyqxmd.com/read/27697042/animal-venom-peptides-potential-for-new-antimicrobial-agents
#17
Muriel Primon-Barros, Alexandre José Macedo
Microbial infections affect people worldwide, causing diseases with significant impact on public health, indicating the need for research and development of new antimicrobial agents. Animal venoms represent a vast and largely unexploited source of biologically active molecules with attractive candidates for the development of novel therapeutics. Venoms consist of complex mixtures of molecules, including antimicrobial peptides (AMPs). Since the discovery of AMPs, they have been studied as promising new antimicrobial drugs...
September 30, 2016: Current Topics in Medicinal Chemistry
https://www.readbyqxmd.com/read/27687600/-venoms-and-medical-research
#18
REVIEW
Frédéric Ducancel
Animal venoms are complex chemical cocktails, comprising a wide range of biologically active reticulated peptides that target with high selectivity and efficacy a variety of enzymes, membrane receptors, ion channels...Venoms can therefore be seen as large natural libraries of biologically active molecules that are continuously selected and highly refined by the evolution process, up to the point where every molecule is endowed with pharmacological properties that are highly valuable in the context of human use and drug development...
2016: Biologie Aujourd'hui
https://www.readbyqxmd.com/read/27617429/a-minimized-human-insulin-receptor-binding-motif-revealed-in-a-conus-geographus-venom-insulin
#19
John G Menting, Joanna Gajewiak, Christopher A MacRaild, Danny Hung-Chieh Chou, Maria M Disotuar, Nicholas A Smith, Charleen Miller, Judit Erchegyi, Jean E Rivier, Baldomero M Olivera, Briony E Forbes, Brian J Smith, Raymond S Norton, Helena Safavi-Hemami, Michael C Lawrence
Insulins in the venom of certain fish-hunting cone snails facilitate prey capture by rapidly inducing hypoglycemic shock. One such insulin, Conus geographus G1 (Con-Ins G1), is the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor and assembly of the hormone's hexameric storage form. Removal of this segment (residues B23-B30) in human insulin results in substantial loss of receptor affinity. Here, we found that Con-Ins G1 is monomeric, strongly binds the human insulin receptor and activates receptor signaling...
October 2016: Nature Structural & Molecular Biology
https://www.readbyqxmd.com/read/27586281/venom-peptides-from-cone-snails-pharmacological-probes-for-voltage-gated-sodium-channels
#20
B R Green, B M Olivera
The venoms of cone snails provide a rich source of neuroactive peptides (conotoxins). Several venom peptide families have been identified that are either agonists (ι- and δ-conotoxins) or antagonists (μ- and μO-conotoxins) of voltage-gated sodium channels (VGSCs). Members of these conotoxin classes have been integral in identifying and characterizing specific neurotoxin binding sites on the channel. Furthermore, given the specificity of some of these peptides for one sodium channel subtype over another, conotoxins have also proven useful in exploring differences between VGSC subtypes...
2016: Current Topics in Membranes
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