Journal
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Volume 92, Issue -, Pages 194-201Publisher
ELSEVIER
DOI: 10.1016/j.ijbiomac.2016.07.032
Keywords
Parkia lectin; Crystal structure; Biological effects
Funding
- Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Fundacao Cearense de Apoio ao Desenvolvimento Cientifico e Tecnologico (FUNCAP)
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The relation structure-activity of the Mimosoideae lectins of Parkia platycephala (PPL) and Parkia biglobosa (PBL) was analyzed in this study. PBL was solved by X-ray crystallography at a resolution of 2.1 angstrom, and the crystal structure belonged to the C222(1) space group. Structural organization and binding sites were also characterized. Specifically, PBL monomer consists of three beta-prism domains tandemly arranged with each one presenting a different carbohydrate recognition domain (CRD). PPL showed antinociceptive activity in the mouse model of acetic acid-induced writhes with maximal inhibitory effect by 74% at I mg/mL. PPL also demonstrated anti-inflammatory effect causing inhibition of leukocyte migration induced by both direct and indirect chemoattractants. These PPL activities were compared to that of PBL described previously. Molecular docking of both PBL and PPL demonstrated some differences in carbohydrate-lectin interaction energy. Comparing structure and biological effects of the two lectins provided new data about their structure and the relation with its biological activities. (C) 2016 Elsevier B.V. All rights reserved.
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