Functionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors synthesis characterization and molecular docking studies
Yükleniyor...
Dosyalar
Tarih
2016
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Bioorganic & Medicinal Chemistry
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Paraoxonase (PON) is a key enzyme in metabolism of living organisms and decreased activity of PON1
was acknowledged as a risk for atherosclerosis and organophosphate toxicity. The present study
describes the synthesis, characterization, PON1 inhibitory properties and molecular docking studies of
functionalized imidazolium and benzimidazolium salts (1a–5g). The structures of all compounds were
elucidated by IR, NMR, elemental analysis and structures of compounds 2b and 2c were characterized
by single-crystal X-ray diffraction. Compound 1c, a coumarin substituted imidazolium salt showed the
best inhibitory effect on the activity of PON1 with good IC50 value (6.37 lM). Kinetic investigation was
evaluated for this compound and results showed that this compound is competitive inhibitor of PON1
with Ki value of 2.39 lM. Molecular docking studies were also performed for most active compound 1c
and one of least active compound 2c in order to determine the probable binding model into active site
of PON1 and validation of the experimental results.
Açıklama
Anahtar Kelimeler
Benzimidazolium, Coumarin, Imidazolium, Inhibition, Molecular docking, Paraoxonase 1
Kaynak
Bioorganic & Medicinal Chemistry
WoS Q Değeri
Scopus Q Değeri
Cilt
24
Sayı
6
Künye
Karataş, M. O. Uslu, H. Alıcı, B. Gökçe, B. Gençer, N. Arslan, O. Arslan, N. B. Özdemir, N. (2016). Functionalized imidazolium and benzimidazolium salts as paraoxonase 1 inhibitors Synthesis characterization and molecular docking studies. Bioorganic & Medicinal Chemistry, 24(6), 1392–1401.
