An empirical comparison of stock market bubbles

Korkmaz, Özge; Bari, Bilgin; Adalı, Zafer

doi:10.15295/bmij.v9i4.1889

Cited by 5 publications

(14 citation statements)

References 22 publications

(29 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It was depicted a difference between the affinity values of compounds 3 b (−9.4 kcal/mol) and 3 d (−9.1 kcal/mol), which show the best affinity values in vitro studies, and the affinity values of compound 3 c (−10.7 kcal/mol) (Table 6). All amino acid interactions of 3 b and 3 d compounds, which have higher efficiency in vitro studies, with pancreatic lipase were observed the same compared to the standard orlistat for in silico studies [30] . Therefore, from this point of view, it might explainable why pancreatic lipase and compounds 3 b and 3 d have high efficacy in vitro studies.…”

Section: Resultsmentioning

confidence: 66%

See 1 more Smart Citation

In Vitro and In Silico Evaluation of Amylase, Tyrosinase, and Pancreatic Lipase Inhibitions of Novel Benzothiazole‐Sulfonate Derivatives

Korkmaz,

Bursal,

Kurtay

2023

ChemistrySelect

View full text Add to dashboard Cite

This paper provides a comprehensive account of the synthesis and assessment of newly developed aryl sulfonate derivatives based on benzothiazole as enzyme inhibitors, specifically focusing on their ability to target tyrosinase, amylase, and pancreatic lipase. The assessments were performed utilizing experimental (in vitro) and computational (in silico) methodologies. For this aim, nine different aryl sulfonate derivatives were synthesized. The synthesized compounds were subjected to structural characterizations by utilizing Nuclear Magnetic Resonance (1H NMR, 13C NMR) and High‐Resolution Mass Spectrometry (HRMS) studies, which provided confirmation of their structural properties. The inhibitory efficiency of the compounds was determined by measuring their 50 % inhibitory concentration (IC50) values and comparing them with the standard inhibitory compounds. According to the in vitro amylase activity, benzo[d]thiazol‐2‐yl 4‐methylbenzenesulfonate showed the best inhibition with the lowest IC50 value (43.31±4.3 μM) which was calculated to be at a close level to the IC50 value of standard acarbose (38.50±3.8 μM). Also, benzo[d]thiazol‐2‐yl 4‐bromobenzenesulfonate (22.73±4.15 μM) and benzo[d]thiazol‐2‐yl 4‐chlorobenzenesulfonate (25.28±1.95 μM) were calculated to have the lowest IC50 values and the most effective inhibition capacities against pancreatic lipase. Benzo[d]thiazol‐2‐yl 4‐fluorobenzenesulfonate and benzo[d]thiazol‐2‐yl 4‐methylbenzenesulfonate significantly exhibited superior tyrosinase inhibition compared to other derivatives and conventional kojic acid. In silico molecular docking affirmed that benzo[d]thiazol‐2‐yl naphthalene‐2‐sulfonate presented the highest binding affinities to the studied enzymes, with values of −7.8 kcal/mol for tyrosinase, −10.7 kcal/mol for pancreatic lipase, and −9.4 kcal/mol for α‐amylase. The pharmacokinetic characteristics and drug‐likeness of the synthesized sulfonate derivatives were also evaluated using absorption, distribution, metabolism, excretion, and toxicity (ADMET) prediction. Density Functional Theory (DFT) calculations were employed at the DFT/B3LYP/6‐311 g(d,p) level of theory to investigate the electronic characteristics of the compounds, therefore facilitating the comprehension of the reported enzyme inhibitory actions. In summary, our research highlights the potential of benzothiazole aryl sulfonate derivatives as effective enzyme inhibitors that hold promise for therapeutic applications.

show abstract

Section: Resultsmentioning

confidence: 66%

“…The molecular docking studies for the benzothiazole‐sulfonate hybrid derivatives ( 3 a – i ) was executed in line with protocols previously established [30,48–50] . The target proteins for our docking studies were sourced from the Protein Data Bank.…”

Section: Experimental Studiesmentioning

confidence: 99%

In Vitro and In Silico Evaluation of Amylase, Tyrosinase, and Pancreatic Lipase Inhibitions of Novel Benzothiazole‐Sulfonate Derivatives

Korkmaz,

Bursal,

Kurtay

2023

ChemistrySelect

View full text Add to dashboard Cite

show abstract

“…Compound 5 b was found to have similar interactions with orlistat in terms of bond structure and bond distance. The interactions of compound 5 b with pancreatic lipase were found to be similar compared to orlistat interaction as eleven amino acids [28] . While there were four conventional hydrogen bonds among the bond types formed by Orlistat, compound 5 b did not have conventional hydrogen bonds (Table 2).…”

Section: Resultsmentioning

confidence: 89%

“…The inhibitory effect of benzothiazole‐sulfonate hybrid derivatives containing the azomethine motif ( 5 a – i ) on the pancreatic lipase (PDB ID:1ETH) enzyme was determined by comparison with Orlistat as a standard. While the affinity of orlistat to the enzyme was calculated as −7.1 kcal/mol, [28] the affinity values of the benzothiazole‐sulfonate hybrid derivatives ( 5 a – i ) to the pancreatic lipase enzyme were found as −8.9, −8.7, −8.6, −9.1, −8.7, −8.9, −8.5, −8.8, and −8.6 kcal/mol, respectively. The order of affinity values for all compounds was observed to be 5 d>5 a=5 f>5 h>5 b=5 e>5 c=5 i>5 g>orlistat , respectively.…”

Section: Resultsmentioning

confidence: 99%

“…Thanks to molecular docking applications being frequently preferred in terms of revealing interactions between proteins and ligands, molecular docking studies are of great interest to researchers [25–27] . Root Mean Square Deviation (RMSD) of standards with pancreatic lipase (tetraethylene glycol monooctyl ether) value was calculated in our previous study and used for validation in this study [28] …”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

In Silico and in Vitro Biological Evaluation of Novel Serial Sulfonate Derivatives on Pancreatic Lipase Activity

Yetişsin,

Korkmaz,

Kaya

2023

Chemistry & Biodiversity

View full text Add to dashboard Cite

The novel benzothiazole sulfonate hybrid derivatives containing azomethine group were synthesized and characterized using 1H NMR, 13C NMR, and HRMS analysis. The potential enzyme inhibition activities against pancreatic lipase of the novel benzothiazole sulfonate hybrid derivatives containing azomethine group were screened with in vitro and in silico methods. IC50 values of compounds 5b (23.89 µM), 5i (28.87 µM), and 5f (30.13±4.32) were found to be more effective pancreatic lipase inhibitors than orlistat (57.75 µM) in vitro studies. Also, the binding affinities of compounds 5b (‐8.7 kcal/mol), 5i (‐8.6 kcal/mol), and 5f (‐8.9 kcal/mol) were found potential inhibitors for pancreatic lipase in silico studies. In addition, the absorption distribution, metabolism, and excretion properties (ADME), molecular properties, toxicity estimation, and bioactivity scores of the synthesized compounds were scanned. It was found to have the ability to cross the brain‐blood barrier for compounds 5a, 5b, 5c, and 5d. All compounds were calculated to be taken orally as drugs, suitable for absorption in the intestinal tract and not carcinogenic, as well as very strongly bound to plasma proteins. Finally, compound 5f was observed to be the best inhibitor for pancreatic lipase according to in vitro and in silico studies.

show abstract

Design, Synthesis, Characterization, Enzyme Inhibition, Molecular Docking, and Pharmacological Evaluation of New Chalcone‐Sulfonate Derivatives Bearing Thiophene

Aslan,

Yetişsin,

Korkmaz

et al. 2024

ChemistrySelect

View full text Add to dashboard Cite

The novel chalcone‐sulfonate derivatives bearing thiophene motif were synthesized and characterized using 1H NMR, 13C NMR, and HRMS analysis. The evaluation of in vitro and in silico potential pancreatic lipase inhibition activity of the novel chalcone‐sulfonate derivatives bearing thiophene motif was scanned. IC50 values of compounds 5 i (28.76±2.11 μM) and 5 f (30.58±0.45 μM) were determined to be more effective pancreatic lipase inhibitors for in vitro studies. The best potential inhibitor for pancreatic lipase binding affinity was found as compound 5 f (−9.8 kcal mol−1) for in silico studies. Although compounds 5 f and 5 i were identified as the best pancreatic lipase inhibitor candidates in vitro and molecular docking studies, compounds 5 f and 5 i were predicted mutagenic and carcinogenic properties in mice according to ADMET studies. Deeply, compound 5 h was a more effective pancreatic lipase inhibitor according to enzyme inhibition, molecular docking, and ADMET studies. It can be said that compound 5 h may be a more efficient drug candidate than orlistat in the treatment of obesity.

show abstract

An empirical comparison of stock market bubbles

Cited by 5 publications

References 22 publications

In Vitro and In Silico Evaluation of Amylase, Tyrosinase, and Pancreatic Lipase Inhibitions of Novel Benzothiazole‐Sulfonate Derivatives

In Vitro and In Silico Evaluation of Amylase, Tyrosinase, and Pancreatic Lipase Inhibitions of Novel Benzothiazole‐Sulfonate Derivatives

In Silico and in Vitro Biological Evaluation of Novel Serial Sulfonate Derivatives on Pancreatic Lipase Activity

Design, Synthesis, Characterization, Enzyme Inhibition, Molecular Docking, and Pharmacological Evaluation of New Chalcone‐Sulfonate Derivatives Bearing Thiophene

Contact Info

Product

Resources

About