Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
11026179 | Archives of Biochemistry and Biophysics | 2018 | 34 Pages |
Abstract
Plant ribosome-inactivating proteins (RIPs) are a family of toxins that inhibit protein synthesis. In this study, we have isolated a novel type 2 ribosome-inactivating protein (RIP) present in seeds of the Abrus fruticulosus, named of fruticulosin. Fruticulosin, shows characteristics common to other type 2 RIPs, as specificity by galactosides (d-galactose, N-acetyl-d-galactosamine, and d-lactose), mass of approximately 60â¯kDa and presence of the of disulfide bonds. The N-terminal amino acid sequence (26 residues) of A-chain fruticulosin, determined by Edman degradation, revealed high similarity of the A-chain with those of other type 2 RIPs. The secondary structure of fruticulosin was analysed by circular dichroism, which showed that fruticulosin contains α-helices (22.3%), β-sheets (43.5%), and random coils and corners (34.2%). Furthermore, fruticulosin showed high toxicity in Artemia sp. (3.12â¯Î¼g/mL), inhibited in vitro protein synthesis by a cell-free system and showed RNA N-glycosidase activity. Fruticulosin presented biological activities such as agglutination and antileishmanial activity on promastigote forms of Leishmania major.
Keywords
PBSLPGFITCRLUMTSPMS3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazoliumBSAbovine serum albuminUltravioletSDS-PAGEToxincircular dichroismAntileishmanial activityfluorescein isothiocyanatephenazine methosulphateLipophosphoglycanPhosphate-buffered salinerelative light unit
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Authors
Mayron Alves de Vasconcelos, Samara Sena da Penha, VinÃcius Rodrigues Castro e Silva, Talita Abrante Leite, Elnatan Bezerra de Souza, Bartolomeu Warlene Silva Souza, Edson Holanda Teixeira, André Luis Coelho da Silva,