Anabaenopeptins: What We Know So Far.

Toxins (Basel)

Laboratory of Biotechnology of Enzymes and Biotransformation, Biological Sciences Institute, Federal University of Pará, Belém 66075-110, Brazil.

Published: July 2021

Cyanobacteria are microorganisms with photosynthetic mechanisms capable of colonizing several distinct environments worldwide. They can produce a vast spectrum of bioactive compounds with different properties, resulting in an improved adaptative capacity. Their richness in secondary metabolites is related to their unique and diverse metabolic apparatus, such as Non-Ribosomal Peptide Synthetases (NRPSs). One important class of peptides produced by the non-ribosomal pathway is anabaenopeptins. These cyclic hexapeptides demonstrated inhibitory activity towards phosphatases and proteases, which could be related to their toxicity and adaptiveness against zooplankters and crustaceans. Thus, this review aims to identify key features related to anabaenopeptins, including the diversity of their structure, occurrence, the biosynthetic steps for their production, ecological roles, and biotechnological applications.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402340PMC
http://dx.doi.org/10.3390/toxins13080522DOI Listing

Publication Analysis

Top Keywords

anabaenopeptins cyanobacteria
4
cyanobacteria microorganisms
4
microorganisms photosynthetic
4
photosynthetic mechanisms
4
mechanisms capable
4
capable colonizing
4
colonizing distinct
4
distinct environments
4
environments worldwide
4
worldwide produce
4

Similar Publications

Real-Time Observation of Clickable Cyanotoxin Synthesis in Bloom-Forming Cyanobacteria and .

Toxins (Basel)

December 2024

Research Department for Limnology, University of Innsbruck, Mondseestrasse 9, 5310 Mondsee, Austria.

Recently, the use of click chemistry for localization of chemically modified cyanopeptides has been introduced, i.e., taking advantage of promiscuous adenylation (A) domains in non-ribosomal peptide synthesis (NRPS), allowing for the incorporation of clickable non-natural amino acids (non-AAs) into their peptide products.

View Article and Find Full Text PDF

A cyanobacterial outbreak in Lake Avernus: Targeted and untargeted analyses and follow up actions for food safety.

Chemosphere

December 2024

Department of Chemistry, Istituto Zooprofilattico Sperimentale del Mezzogiorno, via Salute 2, Portici, Naples, 80055, Italy.

A massive Planktothrix rubescens bloom was observed during 2022 in the Lake Avernus, a volcanic lake located in Campania Region (Southern Italy). The cyanobacterial mass migrated, through a channel, to the near Gulf of Pozzuoli, causing the contamination of two marine sites dedicated to mussel farming, thus posing a potential risk for consumers' health. Mussel and water samples, from both the sea and the lake were collected weekly and analyzed by liquid chromatography coupled to tandem mass spectrometry, for identification and quantification of 10 microcystins.

View Article and Find Full Text PDF

Cyanobacteria exhibit a vast diversity from polar to tropical environments. Though much work has been done on elucidating their biodiversity, knowledge on the occurrence, diversity and toxicity of benthic cyanobacteria is limited when compared to the planktonic forms. Integrating molecular techniques with ecological and morphological analyses has become essential in untangling cyanobacterial diversity, particularly for benthic taxa such as the cryptic "Lyngbya.

View Article and Find Full Text PDF
Article Synopsis
  • Cyanobacteria produce various secondary metabolites, including bioactive oligopeptides with unclear functions, particularly from the under-studied species Woronichinia naegeliana.
  • * The oligopeptides cyanopeptolin 1081 and anabaenopeptin 899 are known to negatively impact zooplankton and show structural similarities to related compounds.
  • * Enzyme assays demonstrate that cyanopeptolin 1081 specifically inhibits chymotrypsin and elastase, while anabaenopeptin 899 selectively inhibits carboxypeptidase A, indicating their potential as strong enzyme inhibitors in aquatic environments.*
View Article and Find Full Text PDF

Chemical investigation of the cyanobacterium NIES-4285 led to the isolation of six new natural products, microginins 705 (), 719 (), 733A (), 733B (), and 733C (), and anabaenopeptin 885 (), and three known compounds, anabaenopeptins 871 (), B (), and F (). Planar structures and absolute configurations for - were determined by 2D NMR, HRMS, and Marfey's analyses. Microginin 733C (), and anabaenopeptins 871 () and 885 () contained a unique residue of 2-amino-5-(4-hydroxyphenyl)pentanoic acid (Ahppa): doubly homologated tyrosine (di-hTyr).

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!