Synthesis, inhibition effects, molecular docking and theoretical studies as Paraoxonase 1 (PON1) inhibitors of novel 1,4-dihydropyridine substituted sulfonamide derivatives

Kaya, Mustafa Oguzhan; Demirci, Tuna; Özdemir, Oğuz; Çalışır, Ümit; Sönmez, Fatih; Arslan, Mustafa

doi:10.1007/s00044-023-03029-7

Med Chem Res

2023

DOI: 10.1007/s00044-023-03029-7

|View full text |Cite

Synthesis, inhibition effects, molecular docking and theoretical studies as Paraoxonase 1 (PON1) inhibitors of novel 1,4-dihydropyridine substituted sulfonamide derivatives

Mustafa Oguzhan Kaya

Tuna Demirci

Oğuz Özdemir

et al.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...

Citation Types

Supporting

Mentioning

Contrasting

Year Published

2023

2024

Publication Types

Select...

Article3

Relationship

Self Cite0

Independent3

Authors

Journals

Cited by 3 publications

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

In Vitro Activation of Paraoxonase 1 by Steroids: An Experimental, Molecular Docking, and Molecular Modelling Study

Deveci,

Çıkrıkcı,

Kuru

et al. 2024

ChemistrySelect

View full text Add to dashboard Cite

Paraoxonase 1 (PON1) is an antioxidant enzyme that prevents lipid oxidation by hydrolysing lipid peroxides in the oxidised low‐density lipoprotein (LDL) structure, bound to high‐density lipoprotein (HDL) in serum, and exhibits esterase and lactonase activity. In this work, the hPON1 enzyme was purified from human serum using a hydrophobic gel with Sepharose 4B‐L‐tyrosine‐naphthylamine, and the affinity of some steroid derivatives previously isolated from fungal steroid biotransformations was examined on the pure hPON1 enzyme. The results indicate that all these derivaties activate the hPON1 enzyme to a different extent. Additionally, the binding potential of the most active five steroid derivatives to the PON1 enzyme to form a stable complex was explored through molecular docking and molecular dynamics (MD) simulation. The compounds with the highest potency in the enzymatic assay, S‐8 and S‐20, had the highest binding potential to the enzyme. The stability of the complexes formed by the two compounds was assessed and compared to the stability of the unbound enzyme structure. The enzyme‐compound complexes generally had similar stability to the unbound enzyme structure. Together with this, the MD simulation revealed that compound S‐8 would remain inside the enzyme's binding site during the simulation period, unlike compound S‐20. This situation varies according to the respective derivatives’ functional groups and hydrophobic characteristics.

show abstract

In Vitro Activation of Paraoxonase 1 by Steroids: An Experimental, Molecular Docking, and Molecular Modelling Study

Deveci,

Çıkrıkcı,

Kuru

et al. 2024

ChemistrySelect

View full text Add to dashboard Cite

show abstract

Synthesis, activatory effects, molecular docking and ADME studies as rabbit muscle pyruvate kinase activators of ureido phenyl substituted 1,4-dihydropyridine derivatives

Kaya,

Demirci,

Çalışır

et al. 2023

Res Chem Intermed

View full text Add to dashboard Cite

Rabbit muscle pyruvate kinase activators: Synthesis, molecular docking and theoretical studies of N-substituted sulfonamide derivatives

Kaya,

Demirci,

Musatat

et al. 2024

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Synthesis, inhibition effects, molecular docking and theoretical studies as Paraoxonase 1 (PON1) inhibitors of novel 1,4-dihydropyridine substituted sulfonamide derivatives

Cited by 3 publications

References 45 publications

In Vitro Activation of Paraoxonase 1 by Steroids: An Experimental, Molecular Docking, and Molecular Modelling Study

In Vitro Activation of Paraoxonase 1 by Steroids: An Experimental, Molecular Docking, and Molecular Modelling Study

Synthesis, activatory effects, molecular docking and ADME studies as rabbit muscle pyruvate kinase activators of ureido phenyl substituted 1,4-dihydropyridine derivatives

Rabbit muscle pyruvate kinase activators: Synthesis, molecular docking and theoretical studies of N-substituted sulfonamide derivatives

Contact Info

Product

Resources

About