Structural characterization of a lectin from Canavalia virosa seeds with inflammatory and cytotoxic activities
| Autor: | Ana Paula M. Nascimento, Benildo Sousa Cavada, Renata Morais Ferreira Amorim, Rodrigo B. Leal, Alysson Chaves Almeida, Vanir Reis Pinto-Junior, Bruno A.M. Rocha, Mayara Queiroz Santiago, Celso Shiniti Nagano, Vinicius Jose Da Silva Osterne, Ingrid A.V. Wolin, Adolph Annderson Gonçalves Costa Barreto, J.C. Silva-Filho, Ana Maria Sampaio Assreuy, Plínio Delatorre, Kyria S. Nascimento |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Male Glycan Cell Survival Anti-Inflammatory Agents Crystallography X-Ray Biochemistry 03 medical and health sciences Mice Affinity chromatography Structural Biology Cell Line Tumor Animals Viability assay Amino Acid Sequence Protein Structure Quaternary Molecular Biology Conserved Sequence chemistry.chemical_classification Binding Sites biology Plant Extracts Protein primary structure Lectin Hydrogen Bonding General Medicine Canavalia biology.organism_classification Antineoplastic Agents Phytogenic Rats Molecular Docking Simulation 030104 developmental biology chemistry Sephadex Mannosides Seeds biology.protein Protein Conformation beta-Strand Drug Screening Assays Antitumor Plant Lectins Glycoprotein Protein Binding |
| Zdroj: | International journal of biological macromolecules. 94 |
| ISSN: | 1879-0003 |
| Popis: | A lectin from Canavalia virosa, Diocleinae subtribe, was purified by affinity chromatography with Sephadex G-50 matrix and named ConV. The primary structure of ConV was obtained by mass spectrometry and crystals were obtained by the vapor diffusion method at 293K and belonged to orthorhombic space group P21221 with two molecules in its asymmetric unit. The structure obtained presented Rfactor and Rfree of 18.91% and 24.92% respectively, with no residues in nonallowed regions of Ramachandran plot. The crystal structure was solved at 2.53A and was demonstrated to be very similar to other lectins from the same subtribe. In inflammatory tests, ConV elicited paw edema, but incubation of lectin with glucose beforehand was able to reduce the edematogenic effect, indicating the involvement of the carbohydrate recognition domain in this process. The lectin also showed toxicity to rat C6 glioma cells, disrupting the mitochondrial membrane potential (ΔYm) and decreasing cell viability, indicating an anticancer potential for ConV. In silico studies confirmed that ConV interacts strongly with carbohydrates that comprise the N-glycans of glycoproteins. This finding corroborates the hypothesis which holds that the lectin domain interacts with glycans in molecular targets and that this contributes to the effects observed in biological activities. |
| Databáze: | OpenAIRE |
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