Frutalin Recognizes Complement C3 Over-Expressed by Neoplasms - Abstract
Frutalin (FTL) is a ?-D-galactose-binding lectin obtained from the seeds of Artocarpusincisa L. It has presented several biomedical activities based on the recognition of the carbohydrate binding site. Bioinformatics techniques have sought to elucidate the molecular bases of interaction with biological receptors. Previous studies have demonstrated that Frutalin, in addition to promoting biological activities, is able to recognize differentially expressed glycoproteins in the blood in patients with neoplasms such as breast cancer and acute lymphoblastic leukemia (ALL). The aim of this work was to elucidate the molecular bases of interaction of Frutalin with Complement C3 Protein, a glycoprotein over-expressed in serum of patients with ALL and breast cancer. The possible interaction between FTL with the surface of the complement protein C3 was analyzed using molecular docking, with the Hex 8.0.0 platform. The 10 most energetic clusters were investigated for analysis of interaction energy, binding specificity, CRS-glycoprotein affinity, the amino acids involved and the attraction/repulsion forces. Molecular docking demonstrated high affinity to between FTL and C3 glycans, with high specificity and complexation energy, with 08 hydrogen bonds measuring up to 0.8 angstroms, with high reproducibility. It can be concluded that FTL is a lectin capable of promoting biological and biomedical activities due to the flexibility of its CRS, which allows the recognition of complex glycans present in glycoprotein’s involved in biological phenomena, which makes it a relevant biotechnological tool