<HashMap><database>bioimages</database><scores/><additional><omics_type>Unknown</omics_type><submitter/><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-BIAD1292</full_dataset_link><repository>bioimages</repository><figure_sub>Specimen</figure_sub><figure_sub>Funding</figure_sub><figure_sub>Experiment</figure_sub><figure_sub>Study Component</figure_sub><figure_sub>organisation</figure_sub><figure_sub>Biosample</figure_sub><figure_sub>Associations</figure_sub><figure_sub>Experiments</figure_sub><figure_sub>Image acquisition</figure_sub><pubmed_authors>Martin Offterdinger</pubmed_authors><pubmed_authors>Rainer Kurmayer</pubmed_authors><pubmed_authors>Rubén Morón Asensio</pubmed_authors><pubmed_authors>Anneliese Wiedlroither</pubmed_authors><pubmed_authors>David Schuler</pubmed_authors></additional><is_claimable>false</is_claimable><name>Differential Labelling of Chemically Modified Peptides and Lipids among Cyanobacteria Planktothrix and Microcystis</name><description>The cyanoHAB forming cyanobacteria Microcystis and Planktothrix frequently produce high intracellular amounts of microcystins (MCs) or anabaenopeptins (APs). In this study, chemically modified MCs and APs have been localized on a subcellular level in Microcystis and Planktothrix applying copper-catalyzed alkyne-azide cycloaddition (CuACC). For this purpose, three different non-natural amino acids carrying alkyne or azide moieties were fed to individual P. agardhii strains No371/1 and CYA126/8 as well as to M. aeruginosa strain Hofbauer showing promiscuous incorporation of various amino acid substrates during non-ribosomal peptide synthesis (NRPS). Moreover, CYA126/8 peptide knock-out mutants and non-toxic strain Synechocystis PCC6803 were processed under identical conditions. Simultaneous </description><dates><release>2024-09-29T00:00:00Z</release><modification>2024-08-16T15:29:14.991Z</modification><creation>2024-07-25T15:45:13.144Z</creation></dates><accession>S-BIAD1292</accession><cross_references/></HashMap>