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In vitro acetylcholinesterase inhibition by psoralen using molecular docking and enzymatic studies.

Somani G, Kulkarni C, Shinde P, Shelke R, Laddha K, Sathaye S - J Pharm Bioallied Sci (2015 Jan-Mar)

Bottom Line: Psoralen was found to inhibit AChE enzyme activity in a concentration-dependent manner.Molecular docking study revealed that psoralen binds well within the binding site of the enzyme showing interactions such as π-π stacking and hydrogen bonding with residues present therein.It could be further explored as a potential candidate for further development of new drugs against AD.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmaceutical Sciences and Technology, Pharmacology Research Lab II, Mumbai, Maharashtra, India.

ABSTRACT

Introduction: Alzheimer's disease (AD) has increased at an alarming rate and is now a worldwide health problem. Inhibitors of acetylcholinesterase (AChE) leading to inhibition of acetylcholine breakdown constitute the main therapeutic strategy for AD. Psoralen was investigated as inhibitor of AChE enzyme in an attempt to explore its potential for the management of AD.

Materials and methods: Psoralen was isolated from powdered Psoralea corylifolia fruits. AChE enzyme inhibitory activity of different concentrations of psoralen was investigated by use of in vitro enzymatic and molecular docking studies. Further, the enzyme kinetics were studied using Lineweaver-Burk plot.

Results: Psoralen was found to inhibit AChE enzyme activity in a concentration-dependent manner. Kinetic studies showed psoralen inhibits AChE in a competitive manner. Molecular docking study revealed that psoralen binds well within the binding site of the enzyme showing interactions such as π-π stacking and hydrogen bonding with residues present therein.

Conclusion: The result of AChE enzyme inhibitory activity of the psoralen in this study is promising. It could be further explored as a potential candidate for further development of new drugs against AD.

No MeSH data available.


Related in: MedlinePlus

Lineweaver–Burk plot of anticholinesterase inhibition by different concentrations of the psoralen
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Figure 3: Lineweaver–Burk plot of anticholinesterase inhibition by different concentrations of the psoralen

Mentions: To elucidate the mechanism of AChE inhibition by psoralen, kinetic studies of enzyme activity were performed. Double reciprocal plot of inhibition of ATCI hydrolysis is shown in Figure 3. The relationship between substrate concentration and reaction velocity was in good agreement with Michaelis–Menten equation. The kinetic studies showed that the psoralen showed increased in Km values without much change in the maximum velocity of enzyme activity or Vmax [Table 1]. The kinetic results demonstrated that the mechanism of AChE inhibition was of the competitive nature.


In vitro acetylcholinesterase inhibition by psoralen using molecular docking and enzymatic studies.

Somani G, Kulkarni C, Shinde P, Shelke R, Laddha K, Sathaye S - J Pharm Bioallied Sci (2015 Jan-Mar)

Lineweaver–Burk plot of anticholinesterase inhibition by different concentrations of the psoralen
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4333625&req=5

Figure 3: Lineweaver–Burk plot of anticholinesterase inhibition by different concentrations of the psoralen
Mentions: To elucidate the mechanism of AChE inhibition by psoralen, kinetic studies of enzyme activity were performed. Double reciprocal plot of inhibition of ATCI hydrolysis is shown in Figure 3. The relationship between substrate concentration and reaction velocity was in good agreement with Michaelis–Menten equation. The kinetic studies showed that the psoralen showed increased in Km values without much change in the maximum velocity of enzyme activity or Vmax [Table 1]. The kinetic results demonstrated that the mechanism of AChE inhibition was of the competitive nature.

Bottom Line: Psoralen was found to inhibit AChE enzyme activity in a concentration-dependent manner.Molecular docking study revealed that psoralen binds well within the binding site of the enzyme showing interactions such as π-π stacking and hydrogen bonding with residues present therein.It could be further explored as a potential candidate for further development of new drugs against AD.

View Article: PubMed Central - PubMed

Affiliation: Department of Pharmaceutical Sciences and Technology, Pharmacology Research Lab II, Mumbai, Maharashtra, India.

ABSTRACT

Introduction: Alzheimer's disease (AD) has increased at an alarming rate and is now a worldwide health problem. Inhibitors of acetylcholinesterase (AChE) leading to inhibition of acetylcholine breakdown constitute the main therapeutic strategy for AD. Psoralen was investigated as inhibitor of AChE enzyme in an attempt to explore its potential for the management of AD.

Materials and methods: Psoralen was isolated from powdered Psoralea corylifolia fruits. AChE enzyme inhibitory activity of different concentrations of psoralen was investigated by use of in vitro enzymatic and molecular docking studies. Further, the enzyme kinetics were studied using Lineweaver-Burk plot.

Results: Psoralen was found to inhibit AChE enzyme activity in a concentration-dependent manner. Kinetic studies showed psoralen inhibits AChE in a competitive manner. Molecular docking study revealed that psoralen binds well within the binding site of the enzyme showing interactions such as π-π stacking and hydrogen bonding with residues present therein.

Conclusion: The result of AChE enzyme inhibitory activity of the psoralen in this study is promising. It could be further explored as a potential candidate for further development of new drugs against AD.

No MeSH data available.


Related in: MedlinePlus