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Isolation, Amino Acid Sequence and Biological Activities of Novel Long‐Chain Polyamine‐Associated Peptide Toxins from the Sponge Axinyssa aculeata
Author(s) -
Matsunaga Satoko,
Jimbo Mitsuru,
Gill Martin B.,
LashVan Wyhe L. Leanne,
Murata Michio,
omura Ken'ichi,
Swanson Geoffrey T.,
Sakai Ryuichi
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201100329
Subject(s) - edman degradation , peptide , polyamine , peptide sequence , biochemistry , sponge , amino acid , biology , residue (chemistry) , biological activity , chemistry , in vitro , botany , gene
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.