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Therapeutically targeting protein–glycan interactions
Author(s) -
Rek A,
Krenn E,
Kungl AJ
Publication year - 2009
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.2009.00226.x
Subject(s) - glycan , computational biology , chemistry , biology , microbiology and biotechnology , computer science , biochemistry , glycoprotein
Glycosylation is the most common form of post‐translational modifications by which oligosaccharide side chains are covalently attached to specific residues of the core protein. Especially O‐linked glycan structures like the glycosaminoglycans were found to contribute significantly to many (patho‐)biological processes like inflammation, coagulation, cancer and viral infections. Glycans exert their function by interacting with proteins thereby changing the structure of the interacting proteins and consequently modulating their function. Given the complex nature of cell‐surface and extracellular matrix glycan structures, this therapeutic site has been neglected for a long time, the only exception being the antithrombin III‐glycan interaction which has been sucessfully targeted by unfractionated and low‐molecular weight heparins for many decades. Due to the recent breakthrough in the ‘–ome’ sciences, among them proteomics and glycomics, protein–glycan interactions became more amenable for therapeutic approaches so that novel inhibitors of this interaction are currently in preclinical and clinical studies. An overview of current approaches, their advantages and disadvantages, is given and the promising potential of pharmacologically interfering with protein–glycan interactions is highlighted here.