Abstract
Lectins are proteins that have the ability to bind specifically and reversibly to carbohydrates and glycoconjugates, without altering the structure of the glycosyl ligand. They are found in organisms such as viruses, plants and humans, and they have been shown to possess important biological activities. The objective of this study was to purify and characterize lectins in the seeds of Clitoria fairchildiana, as well as to verify their biological activities. The results indicated the presence of a lectin (CFAL) in the glutelin acid protein fraction, which agglutinated native rabbit erythrocytes. CFAL was purified by column chromatography ion-exchange, DEAE-Sephacel, which was obtained from a peak of protein retained in the matrix by applying 0.5 M NaCl using the step-wise method. Electrophoretic analysis of this lectin in SDS-PAGE indicated a two band pattern protein molecular mass of approximately 100 and 116 kDa. CFAL proved to be unspecific to all carbohydrates/glycoconjugates in common use for the sugar inhibition test. This lectin showed no significant cytotoxicity to human red blood cells. It was observed that CFAL has anti-inflammatory activity in the paw edema induced by carrageenan model, in which a 64% diminution in edema was observed. Antinociceptive effects were observed for CFAL in the abdominal writhing test (induced by acetic acid), in which increasing doses of the lectin caused reduction in the number of contortions by up to 72%. It was concluded that the purified and characterized lectin from the seeds of Clitoria fairchildiana has anti-inflammatory and antinociceptive activity, and is not cytotoxic to human erythrocytes.
Highlights
Lectins are nonimmune proteins or glycoproteins that have at least one non-catalytic binding site that binds and reversibly to either mono- or oligosaccharides [1,2]
The rabbit erythrocytes membrane has a greater diversity in its carbohydrate composition, in other words, various oligosaccharides and glycoconjugates
A lectin from C. fairchildiana was purified and shown to be a glycoprotein with an electrophoretic pattern consisting of two bands with molecular weights of approximately 100 e 116 kDa
Summary
Lectins are nonimmune proteins or glycoproteins that have at least one non-catalytic binding site that binds and reversibly to either mono- or oligosaccharides [1,2] These proteins are distributed in plants, animals and microorganisms [3]. Our group demonstrated that plant lectins can display either pro- or anti-inflammatory actions depending on the administration route used, via lectin domain interaction [12,14,15,16]. These effects occur through indirect mechanisms, dependent on macrophage activation by lectins, and possibly leading to the release of neutrophilic chemoattractive factors [11,17]. Considering the clear association between inflammatory processes and development of pain, a classical sign of inflammation, our group has recently demonstrated the antinociceptive effect of plant lectins [18,19,20] in models of inflammatory pain, so the purification and verification of biological activity for new lectins reveals properties that can be of great importance in biomedical and pharmaceutical research
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