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DC Field | Value | Language |
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dc.contributor.author | Almeida, Alexandra S. de | - |
dc.contributor.author | Mendonça, Dayara N.M. | - |
dc.contributor.author | Carneiro, Rômulo F. | - |
dc.contributor.author | Pinheiro, Ulisses | - |
dc.contributor.author | Nascimento, Elielton Francisco do | - |
dc.contributor.author | Andrade, Alexandre L. | - |
dc.contributor.author | Vasconcelos, Mayron A. de | - |
dc.contributor.author | Teixeira, Edson H. | - |
dc.contributor.author | Nagano, Celso S | - |
dc.contributor.author | Sampaio, Alexandre H. | - |
dc.date.accessioned | 2024-07-23T12:51:48Z | - |
dc.date.available | 2024-07-23T12:51:48Z | - |
dc.date.issued | 2023 | - |
dc.identifier.citation | ALMEIDA, Alexandra S. de; MENDONÇA, Dayara N.M.; CARNEIRO, Rômulo F.; PINHEIRO, Ulisses ; NASCIMENTO, Elielton Francisco do; ANDRADE, Alexandre L.; VASCONCELOS, Mayron A. de; TEIXEIRA, Edson H.; NAGANO, Celso S.; SAMPAIO, Alexandre H. Purification, biochemical characterization of a lectin from marine sponge Ircinia strobilina and its effect on the inhibition of bacterial biofilms. Anais da Academia Brasileira de Ciências, v. 95, p. 1-14, 2023. Disponíve: Doi: 20220619 DOI 10.1590/0001-3765202320220619. Acesso em: 23 jul. 24. | pt_BR |
dc.identifier.issn | 0001-3765 | - |
dc.identifier.uri | http://repositorio.ufc.br/handle/riufc/77342 | - |
dc.description.abstract | A new lectin from marine sponge Ircinia strobilina, denominated IsL, was isolated by combination of affinity chromatography in Guar gum matrix followed by size exclusion chromatography. IsL was able to agglutinate native and enzymatically treated rabbit erythrocytes, being inhibited by galactosides, such as α-methyl-D-galactopyranoside, β-methyl-D-galactopyranoside and α-lactose. IsL hemagglutinating activity was stable at neutral to alkaline pH, however the lectin loses its activity at 40° C. The molecular mass determinated by mass spectrometry was 13.655 ± 5 Da. Approximately 40% of the primary structure of IsL was determined by mass spectrometry, but no similarity was observed with any protein. The secondary structure of IsL consists of 28% α-helix, 26% β-sheet, and 46% random region, as determined by dichroism circular. IsL was a calcium-dependent lectin, but no significant variations were observed by circular dichroism when IsL was incubated in presence of calcium and EDTA. IsL was not toxic against Artemia nauplii and did not have antimicrobial activity against bacterial cells. However, the IsL was able to significantly inhibit the biofilm formation of Staphylococcus aureus and Staphylococcus epidermidis. | pt_BR |
dc.language.iso | en | pt_BR |
dc.publisher | Anais da Academia Brasileira de Ciências | pt_BR |
dc.rights | Acesso Aberto | pt_BR |
dc.title | Purification, biochemical characterization of a lectin from marine sponge Ircinia strobilina and its effect on the inhibition of bacterial biofilms | pt_BR |
dc.type | Artigo de Periódico | pt_BR |
dc.subject.ptbr | Esponja marinha | pt_BR |
dc.subject.ptbr | Lecitina | pt_BR |
dc.subject.ptbr | Amino ácido - Sequenciamento | pt_BR |
dc.subject.en | Marine sponge | pt_BR |
dc.subject.en | Lectin | pt_BR |
dc.subject.en | Amino acid sequencing | pt_BR |
local.author.lattes | http://lattes.cnpq.br/9392431322008015 | pt_BR |
Appears in Collections: | LABOMAR - Artigos publicados em revistas científicas |
Files in This Item:
File | Description | Size | Format | |
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2023_art_asalmeida.pdf | 814,99 kB | Adobe PDF | View/Open |
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