Lectin obtained from the red seaweed Bryothamnion triquetrum: Secondary structure and anti-inflammatory activity in mice

• Published in: International journal of biological macromolecules Vol. 112; pp. 1122 - 1130
• Main Authors: Fontenelle, Thais Pontes Carvalho, Lima, Glauber Cruz, Mesquita, Jacilane Ximenes, Lopes, José Luiz de Souza, de Brito, Tarcísio Vieira, Vieira Júnior, Francisco das Chagas, Sales, Adriano Bezerra, Aragão, Karoline Saboia, Souza, Marcellus Henrique Loiola Ponte, Barbosa, André Luiz dos Reis, Freitas, Ana Lúcia Ponte
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-06-2018
• Subjects: Animals; Anti-Inflammatory Agents - chemistry; Anti-Inflammatory Agents - pharmacology; Anti-Inflammatory Agents - therapeutic use; Anti-inflammatory effect; Carrageenan; Cell Movement - drug effects; Dextrans; Edema - drug therapy; Edema - pathology; Female; Hemagglutination - drug effects; Hydrogen-Ion Concentration; Interleukin-1beta - biosynthesis; Lectins - chemistry; Lectins - isolation & purification; Lectins - pharmacology; Lectins - therapeutic use; Marine algae; Mice; Peritonitis - drug therapy; Peritonitis - pathology; Peroxidase - antagonists & inhibitors; Peroxidase - metabolism; Protein Structure, Secondary; Rabbits; Rhodophyta - chemistry; Seaweed - chemistry; Spectrometry, Fluorescence; Structural conformation; Temperature; Tumor Necrosis Factor-alpha - biosynthesis; PBS; CD; Structural conformation; NaOH; DEAE-Sephacel; H2O2; IL-1β; MPO; HCl; BSA; MRW; UFC; TNF-α; Marine algae; NaCl; Anti-inflammatory effect; BtL; HU/mL; ELISA
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2018.02.058

Seaweeds are sources of biomolecules with biological activities and pharmacological potential – for example, lectins, a group of proteins that can bind reversibly to carbohydrates or compounds containing them. The aim of this study was to elucidate the structural properties of a lectin extracted from the red seaweed Bryothamnion triquetrum (BtL) and to investigate its anti-inflammatory activity in mice. The lectin was purified by precipitation with ammonium sulfate and ion-exchange chromatography. Its secondary structure and tryptophan (Trp) microenvironment were analyzed by circular dichroism spectroscopy and steady-state fluorescence spectroscopy, respectively. The anti-inflammatory effect was evaluated by means of paw edema induced by carrageenan or dextran, myeloperoxidase activity in paw tissue, and by measurement of leukocyte and neutrophil migration and cytokine quantification in a peritonitis model. The secondary structure of BtL is mostly composed of β-strands and unordered conformation, and it is quite resistant to extremes of pH and temperature, preserving the exposure of Trp residues under these conditions. In an assessment of biological activities, groups of mice were subjected to pretreatment with BtL before the inflammatory stimulus. BtL had anti-inflammatory effects in the models tested, and hence may be considered a molecule with potential to be used in the pharmaceutical industry.