Abstract
Pyrylium salts react exclusively with the ϵ-amino group of lysyl moieties and display a degree of selectivity exceeding all other known amino group reagents. This study represents the first use of a pyrylium salt in positively identifying the functional role of lysyl residues in a biologically active molecule, the Na + glucose cotransporter protein. We synthesized a hydrophilic pyrylium salt, 4-(4-methoxy-3-sulfophenyl)-2,6-bis(4-sulfophenyl)pyrylium perchlorate, which formed a stable pyridinium cation upon reaction with Nα-acetyl-L-lysine methyl ester. This pyrylium inhibited Na + glucose cotransporter activity in purified brush border membranes, in a concentration-dependent manner. The data unequivocally establish that critical lysyl residues are responsible for the activity of the membrane-bound glucose cotransporter protein.
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