Novel Schiff Base Sulfonate Derivatives as Carbonic Anhydrase and Acetylcholinesterase Inhibitors: Synthesis, Biological Activity, and Molecular Docking Insights

Basit Öğe Kaydı
dc.authoridozaslan, muhammet serhat/0000-0002-5060-2048
dc.contributor.authorYasar, Umit
dc.contributor.authorDemir, Yeliz
dc.contributor.authorGonul, Ilyas
dc.contributor.authorOzaslan, Muhammet Serhat
dc.contributor.authorCelik, Gizem Gumusgoz
dc.contributor.authorTurkes, Cuneyt
dc.contributor.authorBeydemir, Sukru
dc.date.accessioned2025-03-18T12:27:46Z
dc.date.available2025-03-17T12:27:46Z
dc.date.issued2025
dc.departmentTarsus Üniversitesi
dc.description.abstractSulfonate derivatives are an essential class of compounds with diverse pharmacological applications. This study presents the synthesis and detailed characterization of six novel Schiff base sulfonate derivatives (L1-L6) through spectroscopic techniques (FT-IR and NMR). Their inhibitory potential was evaluated against human carbonic anhydrase isoenzymes (hCA I and hCA II) and acetylcholinesterase (AChE), which are crucial therapeutic targets for diseases such as glaucoma, epilepsy, and Alzheimer's disease. The KI values for the compounds concerning AChE, hCA I, and hCA II enzymes were in the ranges of 106.10 +/- 14.73 to 422.80 +/- 17.64 nM (THA: 159.61 +/- 8.41 nM), 116.90 +/- 24.40 to 268.00 +/- 35.84 nM (AAZ: 439.17 +/- 9.30 nM), and 177.00 +/- 35.03 to 435.20 +/- 75.98 nM (AAZ: 98.28 +/- 1.69 nM), respectively. Molecular docking analyses revealed key interactions within the active sites of the enzymes, including hydrogen bonding with critical residues and pi-pi stacking interactions. Notably, L3 demonstrated superior inhibition against hCA I (KI: 116.90 +/- 24.40 nM) and AChE (KI: 106.10 +/- 14.73 nM), positioning it as a promising lead compound. This comprehensive investigation contributes to the development of isoform-specific inhibitors for therapeutic use and provides valuable insights into their binding mechanisms. The findings underscore the potential of Schiff base sulfonates as scaffolds in drug discovery for neurodegenerative and metabolic disorders.
dc.description.sponsorshipResearch Fund of Anadolu University [2102S003]
dc.description.sponsorshipThis work was supported by the Research Fund of Anadolu University (grant number 2102S003).
dc.identifier.doi10.1002/cbdv.202402893
dc.identifier.issn1612-1872
dc.identifier.issn1612-1880
dc.identifier.pmid39654314
dc.identifier.scopus2-s2.0-85214421798
dc.identifier.scopusqualityQ3
dc.identifier.urihttps://doi.org/10.1002/cbdv.202402893
dc.identifier.urihttps://hdl.handle.net/20.500.13099/2420
dc.identifier.wosWOS:001390062800001
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherWiley-V C H Verlag Gmbh
dc.relation.ispartofChemistry & Biodiversity
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250316
dc.subjectacetylcholinesterase
dc.subjectcarbonic anhydrase
dc.subjectenzyme inhibition
dc.subjectSchiff bases
dc.titleNovel Schiff Base Sulfonate Derivatives as Carbonic Anhydrase and Acetylcholinesterase Inhibitors: Synthesis, Biological Activity, and Molecular Docking Insights
dc.typeArticle

Dosyalar

Koleksiyon

WoS İndeksli Yayınlar Koleksiyonu
PubMed İndeksli Yayınlar Koleksiyonu
Scopus İndeksli Yayınlar Koleksiyonu