Lectins from Parkia biglobosa and Parkia platycephala: A comparative study of structure and biological effects

被引:14
作者
Bari, Alfa Umaro [1 ]
Santiago, Mayara Queiroz [1 ]
Silva Osterne, Vinicius Jose [1 ]
Pinto-Junior, Vanir Reis [1 ]
Pereira, Livia Paulo [2 ]
Silva-Filho, Jose Caetano [3 ]
Debray, Henri [4 ]
Matias Rocha, Bruno Anderson [5 ]
Delatorre, Plinio [3 ]
Teixeira, Claudener Souza [6 ]
Neto, Cornevile Correia [1 ]
Sampaio Assreuy, Ana Maria [2 ]
Nascimento, Kyria Santiago [1 ]
Cavada, Benildo Sousa [1 ]
机构
[1] Univ Fed Ceara, Dept Bioquim & Biol Mol, Lab Mol Biol Ativas, BioMol Lab, Campus Pici S-N Bloco 907, BR-60440970 Fortaleza, Ceara, Brazil
[2] Univ Estadual Ceara, Inst Super Ciencias Biomed, Lab Fisiofarmacol Inflamacao, BR-60714242 Fortaleza, Ceara, Brazil
[3] Univ Fed Paraiba, Dept Biol Mol, BR-58059900 Joao Pessoa, Paraiba, Brazil
[4] Univ Sci & Technol, Lille, France
[5] Univ Fed Ceara, Dept Bioquim & Biol Mol, Campus Pici S-N Bloco 907, BR-60440970 Fortaleza, Ceara, Brazil
[6] Univ Fed Maranhao, Ctr Ciencias Agr & Ambientais, Maranhao, Brazil
关键词
Parkia lectin; Crystal structure; Biological effects; QUATERNARY ARRANGEMENT; CRYSTAL-STRUCTURE; PURIFICATION; SPECIFICITY; MANNOSE; REVEALS; PROTEINS; JACALIN; SEEDS;
D O I
10.1016/j.ijbiomac.2016.07.032
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:194 / 201
页数:8
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