Peptide fingerprinting of the sea anemone Heteractis magnifica mucus revealed neurotoxins, Kunitz-type proteinase inhibitors and a new ß-defensin α-amylase inhibitor.
J Proteomics
; 173: 12-21, 2018 02 20.
Article
em En
| MEDLINE
| ID: mdl-29191747
ABSTRACT
Sea anemone mucus, due to its multiple and vital functions, is a valuable substance for investigation of new biologically active peptides. In this work, compounds of Heteractis magnifica mucus were separated by multistage liquid chromatography and resulting fractions were analyzed by MALDI-TOF MS. Peptide maps constructed according to the molecular masses and hydrophobicity showed presence of 326 both new and known peptides. Several major peptides from mucus were identified, including the sodium channel toxin RpII isolated earlier from H. magnifica, and four Kunitz-type proteinase inhibitors identical to H. crispa ones. Kunitz-type transcript diversity was studied and sequences of mature peptides were deduced. New ß-defensin α-amylase inhibitor, a homolog of helianthamide from Stichodactyla helianthus, was isolated and structurally characterized. Overall, H. magnifica is a source of biologically active peptides with great pharmacological potential. BIOLOGICAL SIGNIFICANCE:
Proteinase and α-amylase inhibitors along with toxins are major components of H. magnifica mucus which play an important role in the successful existence of sea anemones. Obtained peptide maps create a basis for more accurate identification of peptides during future transcriptomic/genomic studies of sea anemone H. magnifica.Palavras-chave
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Anêmonas-do-Mar
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Mapeamento de Peptídeos
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Muco
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article