Kucukbay, F. ZehraKucukbay, HasanTanc, MuhammetSupuran, Claudiu T.2024-08-042024-08-0420161475-63661475-6374https://doi.org/10.3109/14756366.2015.1113173https://hdl.handle.net/11616/97518N-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.eninfo:eu-repo/semantics/openAccessCarbonic anhydrasecoumarininhibitorN-protected amino acid derivativesArticle316119812022658625410.3109/14756366.2015.11131732-s2.0-84989332094Q1WOS:000385270300042Q1