galectin-6 Inibidores

Os inibidores comuns da galectina-6 incluem, entre outros, o TD-139 CAS 1450824-22-2, a 4-fenilbutilamina CAS 13214-66-9, a castanospermina CAS 79831-76-8, a desoxinojirimicina CAS 19130-96-2 e o cloridrato de desoxianojirimicina CAS 84444-90-6.

Chemical inhibitors of galectin-6 include a variety of compounds that interfere with its ability to interact with glycoprotein targets. TD139, for example, is known to bind to the carbohydrate recognition domain of galectin-3 and, due to structural similarities, can inhibit galectin-6 by preventing it from interacting with its glycoprotein attachments. Similarly, LacNAc (N-acetyllactosamine), a disaccharide, can serve as a competitive inhibitor of galectin-6, mimicking the oligosaccharides to which the protein naturally binds, thus obstructing its binding sites. Thiodigalactoside works on the same principle, resembling the galactoside sugars to which galectin-6 normally adheres, which leads to the blocking of its carbohydrate recognition domain. In addition, Davanat, a modified polysaccharide, can inhibit galectin-6 by binding to its recognition domain, thus preventing its interaction with natural fixatives.

Other inhibitors affect the process of protein glycosylation, which is crucial for the functional interaction of galectin-6 with its glycoprotein targets. Phenylbutylamine can disrupt glycosylation processes, thus reducing the availability of glycosylated proteins for galectin-6 protein binding. Castanospermine and deoxynojirimycin are glucosidase inhibitors that indirectly inhibit galectin-6 by altering protein glycosylation, which leads to a reduction in binding efficiency. Deoxymanojirimycin and suainsonin inhibit mannosidase enzymes, which are also involved in the glycosylation pathway; their inhibition results in poorly glycosylated proteins that galectin-6 cannot recognize effectively. Miglustat acts by inhibiting glucosylceramide synthase, which leads to changes in the synthesis of glycosphingolipids and consequently disrupts the glycosylation patterns recognized by galectin-6. Finally, cytisine, although not a primary inhibitor of galectins, can bind to the carbohydrate recognition domains of galectin-6. Cytisine can occupy these sites, preventing it from interacting with its natural fixatives, resulting in functional inhibition.