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Special Issue "Toxins - Organic and Analytical Chemistry"

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A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: closed (30 November 2010)

Special Issue Editor

Guest Editor
Dr. Jean-Marc Sabatier

Laboratory INSERM UMR 1097, Aix-Marseille University, 163, Parc Scientifique et Technologique de Luminy, Avenue de Luminy, Bâtiment TPR2, Case 939, Marseille 13288, France
E-Mail
Phone: +33 491 82 87 50
Fax: +33 491 83 09 26
Interests: chemical synthesis; peptide synthesis; structure-activity relationships; medicinal chemistry; candidate drugs; antivirals, antibacterials; antioxidants; toxins

Special Issue Information

Dear Colleagues,

Animal venoms are rich sources of potent bioactive molecules. A majority of these are peptides acting on ion channels, cellular receptors, or enzymes. During the last decade, serious efforts have been made to detail the pharmacology of toxins and venom peptides, highlighting their structural and functional diversities, as well as potential value as chemotherapeutic drugs to treat specific human diseases. This special issue of Molecules deals with the various aspects of toxins (and derivatives) from both marine and non-marine environments, including their potential applications in therapy.

Dr. Jean-Marc Sabatier
Guest Editor

Keywords

  • toxinology
  • animal venoms
  • toxins
  • ion channel blockers
  • toxin-derived drug
  • drug design
  • toxin engineering
  • therapy

Related Special Issue

Published Papers (4 papers)

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Research

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Open AccessArticle Lipophilic Toxin Profile in Mytilus galloprovincialis during Episodes of Diarrhetic Shellfish Poisoning (DSP) in the N.E. Adriatic Sea in 2006
Molecules 2011, 16(1), 888-899; doi:10.3390/molecules16010888
Received: 22 November 2010 / Revised: 31 December 2010 / Accepted: 18 January 2011 / Published: 21 January 2011
Cited by 11 | PDF Full-text (274 KB)
Abstract
Dinophysis spp. blooms and related shellfish toxicity events of diarrhetic shellfish poisoning (DSP) have been the most reported toxicity event through the Croatian National monitoring program. With the aim to characterize the DSP toxin profile in shellfish farmed in Croatia, for the first
[...] Read more.
Dinophysis spp. blooms and related shellfish toxicity events of diarrhetic shellfish poisoning (DSP) have been the most reported toxicity event through the Croatian National monitoring program. With the aim to characterize the DSP toxin profile in shellfish farmed in Croatia, for the first time a complete analysis of the toxin profile of Croatian mussels has been carried out using the LC-MS/MS technique. The obtained results showed okadaic acid (OA) as the main toxin contaminating Croatian mussels at that time. The maximum concentration of OA in shellfish tissue was recorded 12 days after the Dinophysis fortii bloom, thus suggesting that rapid growth of the toxin level in the shellfish occurred in the first week after the bloom while it was slower in the second week. Furthermore, the presence of only OA at concentrations which could endanger human health suggests D. fortii as the main organism responsible for the toxic event that occurred in Lim Bay. The presence of gymnodimine and spirolides in Croatian mussel has been detected for the first time, while the presence of yessotoxin and pectenotoxin-2 is confirmed. Full article
(This article belongs to the Special Issue Toxins - Organic and Analytical Chemistry)

Review

Jump to: Research

Open AccessReview Quantitative Mass Spectrometry for Bacterial Protein Toxins — A Sensitive, Specific, High-Throughput Tool for Detection and Diagnosis
Molecules 2011, 16(3), 2391-2413; doi:10.3390/molecules16032391
Received: 14 February 2011 / Revised: 1 March 2011 / Accepted: 9 March 2011 / Published: 14 March 2011
Cited by 26 | PDF Full-text (1625 KB)
Abstract
Matrix-assisted laser-desorption time-of-flight (MALDI-TOF) mass spectrometry (MS) is a valuable high-throughput tool for peptide analysis. Liquid chromatography electrospray ionization (LC-ESI) tandem-MS provides sensitive and specific quantification of small molecules and peptides. The high analytic power of MS coupled with high-specificity substrates is ideally
[...] Read more.
Matrix-assisted laser-desorption time-of-flight (MALDI-TOF) mass spectrometry (MS) is a valuable high-throughput tool for peptide analysis. Liquid chromatography electrospray ionization (LC-ESI) tandem-MS provides sensitive and specific quantification of small molecules and peptides. The high analytic power of MS coupled with high-specificity substrates is ideally suited for detection and quantification of bacterial enzymatic activities. As specific examples of the MS applications in disease diagnosis and select agent detection, we describe recent advances in the analyses of two high profile protein toxin groups, the Bacillus anthracis toxins and the Clostridium botulinum neurotoxins. The two binary toxins produced by B. anthracis consist of protective antigen (PA) which combines with lethal factor (LF) and edema factor (EF), forming lethal toxin and edema toxin respectively. LF is a zinc-dependent endoprotease which hydrolyzes specific proteins involved in inflammation and immunity. EF is an adenylyl cyclase which converts ATP to cyclic-AMP. Toxin-specific enzyme activity for a strategically designed substrate, amplifies reaction products which are detected by MALDI-TOF-MS and LC-ESI-MS/MS. Pre-concentration/purification with toxin specific monoclonal antibodies provides additional specificity. These combined technologies have achieved high specificity, ultrasensitive detection and quantification of the anthrax toxins. We also describe potential applications to diseases of high public health impact, including Clostridium difficile glucosylating toxins and the Bordetella pertussis adenylyl cyclase. Full article
(This article belongs to the Special Issue Toxins - Organic and Analytical Chemistry)
Open AccessReview Small Molecule Inhibitors as Countermeasures for Botulinum Neurotoxin Intoxication
Molecules 2011, 16(1), 202-220; doi:10.3390/molecules16010202
Received: 30 November 2010 / Revised: 20 December 2010 / Accepted: 29 December 2010 / Published: 30 December 2010
Cited by 19 | PDF Full-text (3737 KB)
Abstract
Botulinum neurotoxins (BoNTs) are the most potent of known toxins and are listed as category A biothreat agents by the U.S. CDC. The BoNT-mediated proteolysis of SNARE proteins inhibits the exocytosis of acetylcholine into neuromuscular junctions, leading to life-threatening flaccid paralysis. Currently, the
[...] Read more.
Botulinum neurotoxins (BoNTs) are the most potent of known toxins and are listed as category A biothreat agents by the U.S. CDC. The BoNT-mediated proteolysis of SNARE proteins inhibits the exocytosis of acetylcholine into neuromuscular junctions, leading to life-threatening flaccid paralysis. Currently, the only therapy for BoNT intoxication (which results in the disease state botulism) includes experimental preventative antibodies and long-term supportive care. Therefore, there is an urgent need to identify and develop inhibitors that will serve as both prophylactic agents and post-exposure ‘rescue’ therapeutics. This review focuses on recent progress to discover and develop small molecule inhibitors as therapeutic countermeasures for BoNT intoxication. Full article
(This article belongs to the Special Issue Toxins - Organic and Analytical Chemistry)
Open AccessReview µ-Conotoxins as Leads in the Development of New Analgesics
Molecules 2010, 15(4), 2825-2844; doi:10.3390/molecules15042825
Received: 9 March 2010 / Revised: 6 April 2010 / Accepted: 12 April 2010 / Published: 19 April 2010
Cited by 34 | PDF Full-text (503 KB)
Abstract
Voltage-gated sodium channels (VGSCs) contain a specific binding site for a family of cone shell toxins known as µ-conotoxins. As some VGSCs are involved in pain perception and µ-conotoxins are able to block these channels, µ-conotoxins show considerable potential as analgesics. Recent studies
[...] Read more.
Voltage-gated sodium channels (VGSCs) contain a specific binding site for a family of cone shell toxins known as µ-conotoxins. As some VGSCs are involved in pain perception and µ-conotoxins are able to block these channels, µ-conotoxins show considerable potential as analgesics. Recent studies have advanced our understanding of the three-dimensional structures and structure-function relationships of the µ-conotoxins, including their interaction with VGSCs. Truncated peptide analogues of the native toxins have been created in which secondary structure elements are stabilized by non-native linkers such as lactam bridges. Ultimately, it would be desirable to capture the favourable analgesic properties of the native toxins, in particular their potency and channel sub-type selectivity, in non-peptide mimetics. Such mimetics would constitute lead compounds in the development of new therapeutics for the treatment of pain. Full article
(This article belongs to the Special Issue Toxins - Organic and Analytical Chemistry)
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