Synthesis and carbonic anhydrase inhibitory properties of amino acid - coumarin/quinolinone conjugates incorporating glycine, alanine and phenylalanine moieties
Küçük Resim Yok
Tarih
2016
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Taylor & Francis Ltd
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
N-Protected amino acids (Gly, Ala and Phe) were reacted with amino substituted coumarin and quinolinone derivatives, leading to the corresponding N-protected amino acid-coumarin/quinolinone conjugates. The carbonic anhydrase (CA, EC 4.2.1.1) inhibitory activity of the new compounds was assessed against various human (h) isoforms, such as hCA I, hCA II, hCA IV and hCA XII. The quinolinone conjugates were inactive as enzyme inhibitors, whereas the coumarins were ineffective hCA I/II inhibitors (K(I)s>50 mu M) but were submicromolar hCA IV and XII inhibitors, with inhibition constants ranging between 92 nM and 1.19 mu M for hCA IV, and between 0.11 and 0.79 mu M for hCA XII. These coumarin derivatives, as many others reported earlier, thus show an interesting selective inhibitory profile for the membrane-bound over the cytosolic CA isoforms.
Açıklama
Anahtar Kelimeler
Carbonic anhydrase, coumarin, inhibitor, N-protected amino acid derivatives
Kaynak
Journal of Enzyme Inhibition and Medicinal Chemistry
WoS Q Değeri
Q1
Scopus Q Değeri
Q1
Cilt
31
Sayı
6
