Molecular Modeling of Lectin-Like Protein fromAcacia farnesianaReveals a Possible Anti-Inflammatory Mechanism in Carrageenan-Induced Inflammation

Abstract

Acacia farnesianalectin-like protein (AFAL) is a chitin-binding protein and has been classified as phytohaemagglutinin fromPhaseolus vulgaris(PHA). Legume lectins are examples for structural studies, and this family of proteins shows a remarkable conservation in primary, secondary, and tertiary structures. Lectins have ability to reduce the effects of inflammation caused by phlogistic agents, such as carrageenan (CGN). This paper explains the anti-inflammatory activity of AFAL through structural comparison with anti-inflammatory legume lectins. The AFAL model was obtained by molecular modeling and molecular docking with glycan and carrageenan were performed to explain the AFAL structural behavior and biological activity.Pisum sativumlectin was the best template for molecular modeling. The AFAL structure model is folded as aβsandwich. The model differs from template in loop regions, number ofβstrands and carbohydrate-binding site. Carrageenan and glycan bind to different sites on AFAL. The ability of AFAL binding to carrageenan can be explained by absence of the sixthβ-strand (posteriorβsheets) and twoβstrands in frontal region. AFAL can inhibit pathway inflammatory process by carrageenan injection by connecting to it and preventing its entry into the cell and triggers the reaction.