Uma nova lectina da esponja marinha aplysina sp. (APLYL-1) com atividade citotóxica pra célula tumoral (HeLa) e aglutinante de leishmania amazonensis
A lectin with high binding activity under human erythrocytes of different types of ABO system was isolated from the marine sponge Aplysina sp. by hydroalcoholic extraction and a sequence of purification steps involving gel filtration chromatography on Superdex 75 10/300 GL and ion exchange chromatog...
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| Formato: | Dissertação |
| Idioma: | por |
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| Endereço do item: | https://repositorio.ufrn.br/jspui/handle/123456789/22450 |
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| Resumo: | A lectin with high binding activity under human erythrocytes of different types of ABO system was isolated from the marine sponge Aplysina sp. by hydroalcoholic extraction and a sequence of purification steps involving gel filtration chromatography on Superdex 75 10/300 GL and ion exchange chromatography on Resource Q (FPLC-AKTA Purifier). Once purified, the lectin, named AplyL-1, showed a single peptide chain with a molecular of weight 40 kDa and binding specificity for D-galactose, D-galactosamine and lactose. The AplyL1 hemagglutinating activity was independent of bivalent ions and was not changed in basic conditions (pH > 7.0), but significantly reduced when submitted into acid conditions (pH <7.0). Thermal stability tests showed that AplyL-1 gradually loses its hemagglutinating activity at 40 °C and no longer displays any activity at 100 °C. AplyL-1 has been tested against several tumour cell lines, and howed significantly cytotoxic activity (up to 10 μg/mL) only for human cervical adenocarcinoma cell line (HeLa). For the 3T3 normal cell line no cytotoxic activity was seen. In tests performed with Leishmania braziliensis and Leishmania amazonensis, AplyL-1 exhibited the ability to agglutinate only the species L. amazonensis (at a concentration 77.5 μg/mL). The results show that this new binding galactose derivatives lectin, could be important to development of new products with biotechnological and phylogenetic significance. |
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