Molecular modeling of lectin-like protein from Acacia farnesiana reveals a possible anti-inflammatory mechanism in Carrageenan-induced inflammation.
Acacia farnesiana lectin-like protein (AFAL) is a chitin-binding protein and has been classified as phytohaemagglutinin from Phaseolus 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 sativum lectin was the best template for molecular modeling. The AFAL structure model is folded as a β sandwich. The model differs from template in loop regions, number of β strands 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 sixth β -strand (posterior β sheets) and two β strands 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.
Departamento de Biologia Molecular, Universidade Federal da Paraíba, Campus I, Cidade Universitária, 58059-900 João Pessoa, PB, Brazil.
Vanessa Erika Ferreira
VE
Abrantes
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, BioMol-Lab, Campus do Pici S/N, 60440-970 Fortaleza, CE, Brazil.
Bruno Anderson
BA
Matias da Rocha
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, BioMol-Lab, Campus do Pici S/N, 60440-970 Fortaleza, CE, Brazil.
Raphael
R
Batista da Nóbrega
Departamento de Biologia Molecular, Universidade Federal da Paraíba, Campus I, Cidade Universitária, 58059-900 João Pessoa, PB, Brazil.
José Caetano
JC
Silva-Filho
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, BioMol-Lab, Campus do Pici S/N, 60440-970 Fortaleza, CE, Brazil.
Claudener Souza
CS
Teixeira
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, BioMol-Lab, Campus do Pici S/N, 60440-970 Fortaleza, CE, Brazil.
Benildo Sousa
BS
Cavada
Departamento de Biologia Molecular, Universidade Federal da Paraíba, Campus I, Cidade Universitária, 58059-900 João Pessoa, PB, Brazil.
Carlos Alberto de Almeida
CA
Gadelha
Departamento de Farmacologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, 14049-900 Ribeirão Preto, SP, Brazil.
Sergio Henrique
SH
Ferreira
Departamento de Farmacologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, 14049-900 Ribeirão Preto, SP, Brazil.
Jozi Godoy
JG
Figueiredo
Departamento de Biologia Molecular, Universidade Federal da Paraíba, Campus I, Cidade Universitária, 58059-900 João Pessoa, PB, Brazil.
Tatiane
T
Santi-Gadelha
Departamento de Biologia Molecular, Universidade Federal da Paraíba, Campus I, Cidade Universitária, 58059-900 João Pessoa, PB, Brazil.
Plinio
P
Delatorre
D000045:Acacia; D000818:Animals; D000893:Anti-Inflammatory Agents / Q000737:chemistry* / Q000378:metabolism; D002351:Carrageenan / Q000633:toxicity; D002686:Chitin / Q000737:chemistry; D018360:Crystallography, X-Ray; D007249:Inflammation / Q000139:chemically induced / Q000188:drug therapy* / Q000473:pathology; D051379:Mice; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D010835:Phytohemagglutinins / Q000737:chemistry / Q000378:metabolism; D037121:Plant Lectins / Q000008:administration & dosage / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D011485:Protein Binding
D000893:Anti-Inflammatory Agents; D010835:Phytohemagglutinins; D037121:Plant Lectins; D002686:Chitin; D002351:Carrageenan