{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T17:53:08Z","timestamp":1791913988490,"version":"4.3.4"},"reference-count":77,"publisher":"American Chemical Society (ACS)","issue":"40","license":[{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001711","name":"Schweizerischer Nationalfonds zur F?rderung der Wissenschaftlichen Forschung","doi-asserted-by":"publisher","award":["CRSII5_202290"],"award-info":[{"award-number":["CRSII5_202290"]}],"id":[{"id":"10.13039\/501100001711","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,13]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Harmful cyanobacterial blooms produce diverse bioactive metabolites, cyanopeptides, whose environmental persistence remains uncertain. First, we investigated enzymatic reactions with cyanopeptides as substrates in aquatic systems. The aquatic enzyme pool from the riverine biofilm showed peptidase and oxidase activities. Incubation of cyanopeptides with the natural aquatic enzyme pool revealed novel transformation products (TPs) of two microginins (nostoginin BN741 and microginin FR6) and TPs of anabaenopeptins that also formed when incubated with intact biofilm. Next, we probed underlying mechanisms with peptidases as functional analogs of the aquatic enzyme pool. Carboxypeptidase Y produced identical hydrolysis TPs of the two microginins. A multicopper oxidase rapidly transformed tyrosine-containing microcystins, anabaenopeptins, and microginins, in the presence of the mediator 2,2\u2032-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS). Tyrosine-free congeners remained stable. Lastly, we investigated cyanopeptides as enzyme inhibitors. Cyanopeptolins inhibited trypsin (IC50 = 53.75 nM), chymotrypsin (IC50 = 2.2 \u03bcM), and analogous activities in the aquatic enzyme pool. Anabaenopeptins and microginins showed only mild inhibition of carboxypeptidase Y. As different cyanopeptides are co-produced by cyanobacteria, biotransformation is expected to differ in mixtures compared to single-compound assessments due to the observed inhibition taking place at the same time. Similarly, their release during bloom events may influence the transformation of other organic compounds in surface waters.<\/jats:p>","DOI":"10.1021\/acs.est.6c07305","type":"journal-article","created":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T01:02:05Z","timestamp":1790730125000},"page":"29054-29065","source":"Crossref","is-referenced-by-count":0,"title":["Dual\nRoles of Cyanopeptides as Substrates and Inhibitors\nof Enzymes in Surface Waters"],"prefix":"10.1021","volume":"60","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-0561-8032","authenticated-orcid":true,"given":"Xuejian","family":"Wang","sequence":"first","affiliation":[{"name":"Swiss Federal Institute of Aquatic Science and Technology (EAWAG) , ,","place":["Du\u0308bendorf, Switzerland, 8600"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elena","family":"Lippuner","sequence":"additional","affiliation":[{"name":"Swiss Federal Institute of Aquatic Science and Technology (EAWAG) , ,","place":["Du\u0308bendorf, Switzerland, 8600"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yaochun","family":"Yu","sequence":"additional","affiliation":[{"name":"Swiss Federal Institute of Aquatic Science and Technology (EAWAG) , ,","place":["Du\u0308bendorf, Switzerland, 8600"]},{"name":"Stanford University , , 473 Via Ortega , , ,","place":["Stanford, California, United States, 94305"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5475-6730","authenticated-orcid":true,"given":"Elisabeth M. L.","family":"Janssen","sequence":"additional","affiliation":[{"name":"Swiss Federal Institute of Aquatic Science and Technology (EAWAG) , ,","place":["Du\u0308bendorf, Switzerland, 8600"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,29]]},"reference":[{"issue":"8","key":"2026101310155350800_cit1","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1038\/s41579-018-0040-1","article-title":"Cyanobacterial blooms","volume":"16","author":"Huisman","year":"2018","journal-title":"Nat. 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Lett."},{"issue":"1","key":"2026101310155350800_cit12","doi-asserted-by":"publisher","first-page":"8","DOI":"10.3390\/md14010008","article-title":"Structures\nand Activity of New Anabaenopeptins Produced\nby Baltic Sea Cyanobacteria","volume":"14","author":"Spoof","year":"2016","journal-title":"Mar. Drugs"},{"issue":"1","key":"2026101310155350800_cit13","doi-asserted-by":"publisher","first-page":"32958","DOI":"10.1038\/srep32958","article-title":"Isolation, Co-Crystallization and Structure-Based Characterization\nof Anabaenopeptins as Highly Potent Inhibitors of Activated Thrombin\nActivatable Fibrinolysis Inhibitor (TAFIa)","volume":"6","author":"Schreuder","year":"2016","journal-title":"Sci. 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Technol."},{"issue":"2","key":"2026101310155350800_cit30","doi-asserted-by":"publisher","first-page":"2037","DOI":"10.1021\/acssuschemeng.7b03451","article-title":"Laccase\/Mediator\nSystems: Their Reactivity toward Phenolic Lignin Structures","volume":"6","author":"Hilgers","year":"2018","journal-title":"ACS Sustainable Chem. Eng."},{"key":"2026101310155350800_cit31","doi-asserted-by":"publisher","first-page":"106689","DOI":"10.1016\/j.aquatox.2023.106689","article-title":"Lethal\nand sublethal effects towards zebrafish larvae of microcystins and\nother cyanopeptides produced by cyanobacteria","volume":"263","author":"Torres","year":"2023","journal-title":"Aquat. Toxicol."},{"issue":"1","key":"2026101310155350800_cit32","doi-asserted-by":"publisher","first-page":"26","DOI":"10.1186\/s12302-021-00465-3","article-title":"Phototransformation kinetics of cyanobacterial\ntoxins and secondary metabolites in surface waters","volume":"33","author":"Natumi","year":"2021","journal-title":"Environ. Sci. Eur."},{"key":"2026101310155350800_cit33","doi-asserted-by":"publisher","DOI":"10.5281\/zenodo.7922070","article-title":"Dataset S75: CyanoMetDB-Comprehensive\ndatabase of secondary metabolites from cyanobacteria","volume":"3","author":"Janssen","year":"2023","journal-title":"Zenodo"},{"issue":"4","key":"2026101310155350800_cit34","doi-asserted-by":"publisher","first-page":"2097","DOI":"10.1021\/es5002105","article-title":"Identifying Small Molecules via High\nResolution Mass Spectrometry: Communicating Confidence","volume":"48","author":"Schymanski","year":"2014","journal-title":"Environ. Sci. Technol."},{"issue":"37","key":"2026101310155350800_cit35","doi-asserted-by":"publisher","first-page":"16560","DOI":"10.1021\/acs.est.4c04813","article-title":"Tracking Extensive Portfolio of Cyanotoxins\nin Five-Year Lake Survey and Identifying Indicator Metabolites of\nCyanobacterial Taxa","volume":"58","author":"Wang","year":"2024","journal-title":"Environ. Sci. Technol."},{"issue":"5","key":"2026101310155350800_cit36","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1111\/j.1747-0285.2011.01207.x","article-title":"Metabolic\nStability of Peptidomimetics: N-Methyl and Aza Heptapeptide Analogs\nof a PKB\/Akt Inhibitor","volume":"78","author":"Tal-Gan","year":"2011","journal-title":"Chem. Biol. Drug Des."},{"issue":"9","key":"2026101310155350800_cit37","doi-asserted-by":"publisher","first-page":"625","DOI":"10.1021\/cb7001126","article-title":"Design of Cyclic\nPeptides That Bind Protein Surfaces with Antibody-Like Affinity","volume":"2","author":"Millward","year":"2007","journal-title":"ACS Chem. Biol."},{"key":"2026101310155350800_cit38","doi-asserted-by":"publisher","first-page":"116488","DOI":"10.1016\/j.jpba.2024.116488","article-title":"Cyclic peptides: A powerful instrument for advancing\nbiomedical nanotechnologies and drug development","volume":"252","author":"Martian","year":"2025","journal-title":"J. Pharm. Biomed. 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Sci. Technol."},{"key":"2026101310155350800_cit42","doi-asserted-by":"publisher","first-page":"134595","DOI":"10.1016\/j.jhazmat.2024.134595","article-title":"Inhibit or promote? Trade-off effect of dissolved organic matter\non the laccase-mediator system","volume":"473","author":"Zhang","year":"2024","journal-title":"J. Hazard. Mater."},{"issue":"4","key":"2026101310155350800_cit43","doi-asserted-by":"publisher","first-page":"750","DOI":"10.3390\/catal13040750","article-title":"Application of Laccase Catalysis in Bond Formation\nand Breakage:\nA Review","volume":"13","author":"Lin","year":"2023","journal-title":"Catalysts"},{"issue":"8","key":"2026101310155350800_cit44","doi-asserted-by":"publisher","first-page":"1052","DOI":"10.1139\/v00-099","article-title":"Reactions of the radical cation derived from 2,2\u2019-azinobis(3-ethylbenzothiazoline-6-sulfonic\nacid) (ABTS\u00b7+) with amino acids. Kinetics and mechanism","volume":"78","author":"Aliaga","year":"2000","journal-title":"Can. J. Chem."},{"issue":"12","key":"2026101310155350800_cit45","doi-asserted-by":"publisher","first-page":"1495","DOI":"10.1016\/0041-0101(94)90308-5","article-title":"Use of a colorimetric protein phosphatase inhibition\nassay and enzyme linked immunosorbent assay for the study of microcystins\nand nodularins","volume":"32","author":"An","year":"1994","journal-title":"Toxicon"},{"issue":"10","key":"2026101310155350800_cit46","doi-asserted-by":"publisher","first-page":"1755","DOI":"10.1021\/np049828f","article-title":"Cyanopeptolin 963A, a Chymotrypsin Inhibitor of Microcystis\nPCC 7806","volume":"67","author":"Bister","year":"2004","journal-title":"J. Nat. 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Hydrobiol."},{"issue":"10","key":"2026101310155350800_cit50","doi-asserted-by":"publisher","first-page":"1593","DOI":"10.1021\/np0702436","article-title":"Lyngbyastatins\n5\u20137, Potent Elastase Inhibitors from Floridian Marine Cyanobacteria,\nLyngbya spp","volume":"70","author":"Taori","year":"2007","journal-title":"J. Nat. Prod."},{"issue":"9","key":"2026101310155350800_cit51","doi-asserted-by":"publisher","first-page":"1625","DOI":"10.1021\/np8002172","article-title":"Kempopeptins A and B, Serine Protease\nInhibitors with Different Selectivity Profiles from a Marine Cyanobacterium,\nLyngbya sp","volume":"71","author":"Taori","year":"2008","journal-title":"J. Nat. 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