Glycosides and amino acyl esters of carbohydrates as potent inhibitors of angiotensin converting enzyme

• Published in: European journal of medicinal chemistry Vol. 41; no. 9; pp. 1059 - 1072
• Main Authors: Lohith, K., Vijayakumar, G.R., Somashekar, B.R., Sivakumar, R., Divakar, S.
• Format: Journal Article
• Language: English
• Published: ISSY-LES-MOULINEAUX Elsevier Masson SAS 01.09.2006; Elsevier
• Subjects: ACE inhibition; Amino acyl esters of carbohydrates; Aminoacylation; Angiotensin-Converting Enzyme Inhibitors - chemistry; Angiotensin-Converting Enzyme Inhibitors - pharmacology; Antihypertensive agents; Bioconversions. Hemisynthesis; Biological and medical sciences; Biotechnology; Carbohydrates - chemistry; Carbohydrates - pharmacology; Cardiovascular system; Chemistry, Medicinal; Enzymatic synthesis; Esters - chemistry; Fundamental and applied biological sciences. Psychology; Glycosides; Health. Pharmaceutical industry; IC 50 values; Industrial applications and implications. Economical aspects; Inhibitory Concentration 50; Life Sciences & Biomedicine; Medical sciences; Methods. Procedures. Technologies; Molecular Structure; Other active biomolecules; Peptidyl-Dipeptidase A - metabolism; Pharmacology & Pharmacy; Pharmacology. Drug treatments; Production of active biomolecules; Science & Technology; Structure-Activity Relationship; Enzymatic synthesis; IC 50 values; Glycosides; Amino acyl esters of carbohydrates; ACE inhibition; AMYLOGLUCOSIDASE; amino acyl esters of carbohydrates; IC50 values; LIPASE-CATALYZED SYNTHESIS; ASSAY; enzymatic synthesis; D-GLUCOSIDE; glycosides; PROTEASE; Ketose; Triacylglycerol lipase; Esterases; Disaccharide; Structure activity relation; Peptidyl-dipeptidase A; Glycoside; Chemical synthesis; Acylate; Glucan 1,4-α-glucosidase; Aldose; Enzyme; Benzene derivatives; Enzyme inhibitor; In vitro; Carboxylic ester hydrolases; Primary alcohol; Peptidases; α-Aminoacid; Alditol; Glycosidases; Phenols; Hydrolases; Peptidyl-dipeptidases; Antihypertensive agent; ACE inhibitor; Enzymatic reaction
• ISSN: 0223-5234; 1768-3254
• DOI: 10.1016/j.ejmech.2006.04.005

About 12 glycosides prepared through amyloglucosidase catalysis and 23 amino acyl esters of carbohydrates prepared through lipase catalysis in organic solvents showed angiotensin converting enzyme (ACE) inhibition activity. Both amino acyl esters of carbohydrates and glycosides exhibited IC 50 values for ACE inhibition in the 0.5 mM to 15.7 mM range. Eugenyl- d-glucoside (IC 50: 0.5 ± 0.04 mM), l-isoleucyl- d-glucose (IC 50: 0.7 ± 0.067 mM), vanillyl- d-sorbitol (IC 50: 0.8 ± 0.09 mM), l-histidyl- d-fructose (IC 50: 0.9 ± 0.087 mM), l-tryptophanyl- d-fructose (IC 50: 0.9 ± 0.092 mM), octyl- d-glucoside (IC 50: 1.0 ± 0.093 mM), vanillyl- d-mannoside (IC 50: 1.0 ± 0.089 mM), l-valyl- d-mannitol (IC 50: 1.0 ± 0.092 mM) and l-phenylalanyl- d-glucose (IC 50: 1.0 ± 0.089 mM) were the compounds, which showed the best ACE inhibitory activities.