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.

Coconut antimicrobial peptide-1 (CnAMP1) is a naturally occurring bioactive peptide from green coconut water (Cocos nucifera L.). Although biological activities have been reported, the physiological relevance of these reports remains elusive as it is unknown if CnAMP1 is taken up into intestinal cells. To address this open question, we investigated the cytotoxicity of CnAMP1 in intestinal cells and its cellular uptake into human intestinal cells. Considering the importance of the P-glycoprotein (P-gp) to the intestinal metabolism of xenobiotics, we also investigated the influence of CnAMP1 on P-gp activity and expression. Both cell lines showed intracellular fluorescence after incubation with fluorescein labelled CnAMP1, indicating cellular uptake of the intact or fragmented peptide. CnAMP1 (12.5–400 μmol/L) showed no signs of cytotoxicity in LS180 and differentiated Caco-2 cells and did not affect P-gp expression and activity. Further research is required to investigate the identity of CnAMP1 hydrolysis fragments and their potential biological activities.