A rapid method for the detection of marine toxins was developed using an ultra-performance liquid chromatography (UPLC) system coupled to a latest generation mass spectrometry (MS) system. The analysis of 21 lipophilic marine toxins was achieved on an Acquity C18 column using a water-acetonitrile gradient with a cycle time of 6.6 min, reducing analysis time by more than a factor two compared to HPLC while maintaining peak resolution. Linear ranges, limits of detection and limits of quantification were established for okadaic acid (OA), pectenotoxin-2, azaspiracid-1 (AZA1), yessotoxin, gymnodimine and 13-desmethylspirolide C. The method was found to be accurate when using a triplicate methanolic extraction. Matrix effects were assessed by standard addition of OA and AZA1 in extracts of raw and heat-treated flesh of mussels and oysters. For the analysis of AZA1, the UPLC-MS method was always prone to signal suppression, while for OA analysis signal suppression was observed in extracts of raw shellfish flesh and signal enhancement in extracts of heat-treated flesh. Matrix effects occurring in the method presented are diminished compared to previous studies.
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http://dx.doi.org/10.1016/j.chroma.2007.05.016 | DOI Listing |
J Comput Aided Mol Des
December 2024
Chongqing Key Laboratory of Natural Product Synthesis and Drug Research, School of Pharmaceutical Sciences, Chongqing University, Chongqing, 401331, China.
Conotoxins, being small disulfide-rich and bioactive peptides, manifest notable pharmacological potential and find extensive applications. However, the exploration of conotoxins' vast molecular space using traditional methods is severely limited, necessitating the urgent need of developing novel approaches. Recently, deep learning (DL)-based methods have advanced to the molecular generation of proteins and peptides.
View Article and Find Full Text PDFArch Microbiol
December 2024
Global Leadership School, Handong Global University, Pohang, 37554, South Korea.
Microcystin-LRs (MC-LR) produced by harmful cyanobacterial blooms (HCBs) pose significant hepatotoxic risks to both the environment and public health. Despite the identification and characterization of a limited number of MC-LR degrading bacteria, the challenge of safely removing MC-LRs from freshwater systems without disrupting aquatic ecosystems remains substantial. This study focused on the isolation of lactic acid bacteria from Bapshikhe, a traditional Korean fermented food, and investigated the mechanisms underlying the degradation of MC-LRs by these bacteria.
View Article and Find Full Text PDFBMC Genomics
December 2024
Center for Evolution and Conservation Biology, Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou), Guangzhou, China.
Background: Animal venom systems are considered as valuable model for investigating the molecular mechanisms underlying phenotypic evolution. Stonefish are the most venomous and dangerous fish because of severe human envenomation and occasionally fatalities, whereas the genomic background of their venom has not been fully explored compared with that in other venomous animals.
Results: In this study, we followed modern venomic pipelines to decode the Synanceia verrucosa venom components.
Shokuhin Eiseigaku Zasshi
December 2024
Fisheries Technology Institute, Japan Fisheries Research and Education Agenc.
Recently, an instrumental analysis using LC-MS/MS has been developed and validated for paralytic shellfish toxins (PSTs) and tetrodotoxin (TTX) in bivalve molluscs in Japanese domestic and overseas. The method for 11 PSTs and TTX in scallops was validated in accordance with a previous report and CODEX-STAN. The samples were prepared by adding the standard mixture of PSTs and TTX to scallop (Patinopecten yessoensis) homogenates, extracted with 1% acetic acid and then cleaned up using an ENVI-Carb (250 mg/3 mL) cartridge.
View Article and Find Full Text PDFBiochem Biophys Res Commun
January 2025
Center of Protein Studies, Faculty of Biology, Havana University, Havana, Cuba.
Sticholysin I and II (St I/II) belong to the actinoporins family; these proteins form pores in host cell membranes by binding their N-terminal segment to the membrane, leading to protein-lipid (toroidal) pores. Peptides derived from actinoporins pore-forming domains replicate their folding properties and permeabilizing effects. Despite the advances in understanding how these proteins and peptides mediate pore formation, the role of different N-terminal segments in inducing membrane curvature is still unclear.
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