X-ray structural studies on the molecular recognition of innovative beta-N- and beta-S-galactosides by peanut lectin (Póster)

EMILIANO PRIMO; WALTER GIORDANO; FERNANDO A. GOLDBAUM; SEBASTIÁN KLINKE; KARINA V. MARIÑO; MARÍA L. UHRIG; ALEJANDRO J. CAGNONI; MARÍA E. CANO; JOSÉ KOVENSKY; LISANDRO H. OTERO

Evento online en Twitter (organizadores de México, EEUU, Brasil y otros)

Conferencia; LatinXChem 2020 Twitter Conference; 2020

Foro LatinXChem (https://www.latinxchem.org/)

Carbohydrate-lectin interactions are involved in important cellular recognition processes, including viral and bacterial infections, inflammation, and tumor metastasis. Hence, the structural studies of lectin-synthetic glycan complexes are essential for understanding the lectin recognition processes and the further design of promising chemotheraeutics that interfere with sugar-lectin interactions.Among plant lectins, peanut lectin (PNA) is highly relevant in the glycobiology field, because of its specificity por beta-galactosides, showing high affinity towards the Thomsen-Friedenreich (TF) antigen, a well known tumor-associated carbohydrate antigen. Given this specificity, PNA is one of the most frequently used molecular probes for the recognition of tumor cell-surface O-glycans. Thus, is has been extensively used in glycobiology for inhibition studies with a variety of beta-galactoside and beta-lactoside ligands. Herein, we report the results obtained from an interdisciplinary study, going from the synthesis of hydrolytically stable glycomimetics, namely beta-N- and beta-S-galactosides, to the determination of the crystal structures of their complexes with PNA.