Strong competitive inhibition of porcine pancreatic alpha-amylase by aminodeoxy derivatives of maltose and maltotriose.
The syntheses are described of 6-amino-6-deoxymaltose (2), the 6-amino-6-deoxy (4), 6'-amino-6'-deoxy (6), and 6"-amino-6"-deoxy (8) derivatives of maltotriose, and the methyl alpha- (10) and beta-glycoside (12) and the 1-deoxy derivative (16) of 4. The Ki values (microM) of these competitive inhibitors of porcine pancreatic alpha-amylase were: 2, 88; 4, 1.9; 6, 2.0; 8, 175; 10, 360; 12, 9000; 16, 7600 (cf. 1800 for maltotriose and 3000 for methyl alpha-maltotrioside). The low values for 4 and 6 reflect reinforcement of the normal binding by ionic attraction and, possibly, interaction of the reducing end groups with the protein.
Lehmann
J
J
Institut für Organische Chemie und Biochemie, Universität Freiburg, Germany.
Schmidt-Schuchardt
M
M
Steck
J
J
D000606:Amino Sugars / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D002240:Carbohydrate Sequence; D008320:Maltose / Q000031:analogs & derivatives*; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology; D013552:Swine; D014312:Trisaccharides / Q000737:chemistry*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors* / Q000378:metabolism
D000606:Amino Sugars; D014312:Trisaccharides; C008317:maltotriose; D008320:Maltose; D000516:alpha-Amylases