The synthesis of some beta-lactams and investigation of their metal-chelating activity, carbonic anhydrase and acetylcholinesterase inhibition profiles

dc.contributor.authorTuran, Burhanettin
dc.contributor.authorSendil, Kivilcim
dc.contributor.authorSengul, Emin
dc.contributor.authorGultekin, Mehmet Serdar
dc.contributor.authorTaslimi, Parham
dc.contributor.authorGülçin, İlhami
dc.contributor.authorSupuran, Claudiu T.
dc.contributor.authorTaslimi, Parham
dc.date.accessioned2019-06-13T06:48:19Z
dc.date.available2019-06-13T06:48:19Z
dc.date.created2016
dc.date.issued2016
dc.date.issuedyyyymmdd2016-12
dc.departmentFakülteler, Fen Fakültesi, Biyoteknoloji Bölümü
dc.description.abstractbeta-Lactam antibiotics are a broad class of antibiotics, consisting of all antibiotic agents that contain a beta-lactam ring in their molecular structures. Synthesis of beta-lactam analogs, which are containing dichloride atoms and N-methyl, N-aromatic rings, was achieved by Schiff bases and dichloroketene compounds. All the synthesized imines and beta-lactam analogs were tested against two physiologically relevant carbonic anhydrase isozymes (hCA I and II) and acetylcholinesterase (AChE). They demponstrated effective inhibitory profiles with K-i values in ranging of 3.22-11.18 nM against hCA I, 3.74-10.41 nM against hCA II, and 0.50-1.57 nM against AChE. On the other hand, acetazolamide and dorzolamide clinically used as CA inhibitors, showed K-i value of 170.34 and 129.26nM against hCA I, and 115.43 and 135.67 nM against hCA II, respectively. Also, tacrine used as standard AChE inhibitor showed Ki value of 5.70 nM against AChE.
dc.identifier.doi10.3109/14756366.2016.1170014
dc.identifier.endpage88
dc.identifier.startpage79
dc.identifier.urihttps://hdl.handle.net/11772/1389
dc.identifier.volume31
dc.language.isoen
dc.publisherInforma
dc.relation.ispartofJournal of Enzyme Inhibition and Medicinal Chemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAcetylcholinesterase
dc.subjectSchiff bases
dc.subjectBeta-lactams
dc.subjectCarbonic anhydrase
dc.subjectEnzyme inhibition
dc.subjectEnzyme purification
dc.titleThe synthesis of some beta-lactams and investigation of their metal-chelating activity, carbonic anhydrase and acetylcholinesterase inhibition profiles
dc.typeArticle
dspace.entity.typePublication
relation.isAuthorOfPublicationdadfa319-65b8-4543-92b4-bea49e0139e9
relation.isAuthorOfPublication.latestForDiscoverydadfa319-65b8-4543-92b4-bea49e0139e9

Dosyalar

Lisans paketi

Listeleniyor 1 - 1 / 1
Yükleniyor...
Küçük Resim
İsim:
license.txt
Boyut:
1.71 KB
Biçim:
Item-specific license agreed upon to submission
Açıklama: