Crystal structures of the peanut lectin in the presence of novel beta- and beta-N-galactosides

PRIMO, E. D.; ALEJANDRO JAVIER CAGNONI; KLINKE, S.; MARÍA EMILIA CANO; KARINA V. MARIÑO; GOLDBAUM, F. A.; MARÍA LAURA UHRIG; OTERO, L. H.

Buenos Aires

Simposio; 3rd Argentinian Symposium on Glycobiology; 2019

Carbohydrate-protein interactions are involved in important cellular recognition processes, including viral and bacterial infections, inflammation, and tumor metastasis. Hence, glycoclusters that interfere with these processes are seen as promising chemotherapeutics. Plant lectins are excellent models to explore therecognition features involved. Among them, the peanut lectin (PNA) is very relevant in the glycobiology field, because of its specificity for β-galactosides, showing high affinity towards Thomsen-Friedenreich (TF) antigen, awell-known tumor-associated carbohydrate antigen. Given this specificity, the PNA lectin is one of the most potential molecular probes available for the recognition of tumor cell O-glycans, thus, it has been extensively used in the glycobiology field on inhibition studies, including our own, of a variety of β-galactoside and β- lactoside ligands.