ArticleChembiochem : a European journal of chemical biology2011
Isolation, amino acid sequence and biological activities of novel long-chain polyamine-associated peptide toxins from the sponge Axinyssa aculeata.
Article in Chembiochem : a European journal of chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- Discovery of Ribosomally Synthesized and Post-translationally Modified Knottins from the Deep-Sea SpongeJournal of natural products · 2026Article
- Harnessing Microalgae as Sustainable Cell Factories for Polyamine-Based Nanosilica for Biomedical Applications.Molecules (Basel, Switzerland) · 2025Review
- Indole-Containing Natural Products 2019-2022: Isolations, Reappraisals, Syntheses, and Biological Activities.Molecules (Basel, Switzerland) · 2022Review
- Fukuyama reduction, Fukuyama coupling and Fukuyama-Mitsunobu alkylation: recent developments and synthetic applications.Molecular diversity · 2022Review
- Cellulose intrafibrillar mineralization of biological silica in a rice plant.Scientific reports · 2021Article
- Soritesidine, a Novel Proteinous Toxin from the Okinawan Marine SpongeMarine drugs · 2019Article
- Cytotoxic Compounds Derived from Marine Sponges. A Review (2010-2012).Molecules (Basel, Switzerland) · 2017Review
- Alkyl chain modulated cytotoxicity and antioxidant activity of bioinspired amphiphilic selenolanes.Toxicology research · 2016Article
- Isolation of novel prototype galectins from the marine ball sponge Cinachyrella sp. guided by their modulatory activity on mammalian glutamate-gated ion channels.Glycobiology · 2013Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
A novel family of functionalized peptide toxins, aculeines (ACUs), was isolated from the marine sponge Axinyssa aculeate. ACUs are polypeptides with N-terminal residues that are modified by the addition of long-chain polyamines (LCPA). Aculeines were present in the sponge extract as a complex mixture with differing polyamine chain lengths and peptide structures. ACU-A and B, which were purified in this study, share a common polypeptide chain but differ in their N-terminal residue modifications. The amino acid sequence of the polypeptide portion of ACU-A and B was deduced from 3' and 5' RACE, and supported by Edman degradation and mass spectral analysis of peptide fragments. ACU induced convulsions upon intracerebroventricular (i.c.v.) injection in mice, and disrupted neuronal membrane integrity in electrophysiological assays. ACU also lysed erythrocytes with a potency that differed between animal species. Here we describe the isolation, amino acid sequence, and biological activity of this new group of cytotoxic sponge peptides.
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