Investigation of In Vitro Inhibitory Effects of Some Carnozole and Carnosic Acid Derivatives Bases On Acetylcholinesterase, Butyrylcholinesterase and Carbonic Anhydrase Isoenzymes


Köksal Z.

EJONS 12, Paris, France, 09 July 2021, pp.1-3

  • Publication Type: Conference Paper / Summary Text
  • City: Paris
  • Country: France
  • Page Numbers: pp.1-3

Abstract

The place and beneficial properties of many natural phenolic compounds such as polyphenols directly in human nutrition are primarily associated with their antioxidant activities. It is known that polyphenolic compounds are obtained from natural products. Carnozole and carnosic acid derivatives are important natural antioxidants found in rosemary (Rosmarinus officinalis). Rosemary is an important medicinal-aromatic plant species and has many biological effects such as antimicrobial, antioxidant, antiviral, and immune system improvement. In this study, in vitro inhibition kinetics of some enzymes (hCA I, hCA II, AChE and BChE) will be investigated on these derivatives (carnosol, carnosic acid, isorosmanol, 12-methoxycarnosic acid, 7-methylrosmanol) whether they have inhibition and activation effects.. Acetylcholinesterase (AChE, EC 3.1.1.7) is known to be abundant in the muscle, brain and erythrocyte membrane, and butyrylcholinesterase (BChE, EC 3.1.1.8) has a higher activity in liver, intestine, heart, kidney and lung. Carbonic anhydrases (CAs, EC 4.2.1.1) is a metalloenzyme containing Zn+2 ions found in all organisms. It is a very important enzyme that plays a role in many physiological events such as acid-base balance, ion exchange, regulation of the cardiovascular system, as well as providing the dissolution of CO2 formed during respiration in water, its transport and removal from the bodythe hydration of carbon dioxide (CO2) to bicarbonate (HCO3 ) and protons (H+), with a high efficiency.

According to the results of this study some inhibition parameters including IC50 and Ki values were determined on hCA I, II, AChE and BChE. The compounds IC50 values in the range of 0.615 to 4.814 µM against hCA I, 4.213 to 5.478 µM against hCA II, 0.704 to 0.9833 µM against AChE and 0.632 to 1.605 µM against BChE. Ki values were in the range of 12.40 ± 7.10 to 462.35 ± 44.42 nM against hCA I, 35.77 ± 3.04 to 330.08 ± 62.23 nM against hCA II, 23.00 ± 25.53 to 357.00 ± 4.02 nM against AChE and 20.00 ± 35.53 to 557.00 ± 4.02 nM against BChE. These Carnozole and Carnosic Acid Derivatives had showed strongest inhibition effects on these enzymes.