| Autor: |
Cavada BS; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Pinto-Junior VR; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil.; Departamento de Física, Universidade Federal do Ceará, Fortaleza, Brazil., Osterne VJS; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil.; Departamento de Nutrição, Universidade Estadual do Ceará, Fortaleza, Brazil., Oliveira MV; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Silva IB; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil., Laranjeira EPP; Instituto Superior de Ciências Biomédicas, Universidade Estadual Do Ceará, Fortaleza, Brazil., Pires AF; Instituto Superior de Ciências Biomédicas, Universidade Estadual Do Ceará, Fortaleza, Brazil., Domingos JLC; Departamento de Física, Universidade Federal do Ceará, Fortaleza, Brazil., Ferreira WP; Departamento de Física, Universidade Federal do Ceará, Fortaleza, Brazil., Sousa JS; Departamento de Física, Universidade Federal do Ceará, Fortaleza, Brazil., Assreuy AMS; Instituto Superior de Ciências Biomédicas, Universidade Estadual Do Ceará, Fortaleza, Brazil., Nascimento KS; Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil. |
| Abstrakt: |
Lectins are a class of proteins or glycoproteins capable of recognizing and interacting with carbohydrates in a specific and reversible manner. Owing to this property, these proteins can interact with glycoconjugates present on the cell surface, making it possible to decipher the glycocode, as well as elicit biological effects, such as inflammation and vasorelaxation. Here, we report a structural and biological study of the mannose/glucose-specific lectin from Dioclea lasiophylla seeds, DlyL. The study aimed to evaluate in detail the interaction of DlyL with Xman and high-mannose N -glycans (MAN3, MAN5 and MAN9) by molecular dynamics (MD) and the resultant in vitro effect on vasorelaxation using rat aortic rings. In silico analysis of molecular docking was performed to obtain the initial coordinates of the DlyL complexes with the carbohydrates to apply as inputs in MD simulations. The MD trajectories demonstrated the stability of DlyL over time as well as different profiles of interaction with Xman and N -glycans. Furthermore, aortic rings assays demonstrated that the lectin could relax pre-contracted aortic rings with the participation of the carbohydrate recognition domain (CRD) and nitric oxide (NO) when endothelial tissue is preserved. These results confirm the ability of DlyL to interact with high-mannose N -glycans with its expanded CRD, supporting the hypothesis that DlyL vasorelaxant activity occurs primarily through its interaction with cell surface glycosylated receptors.Communicated by Ramaswamy H. Sarma. |
