Biological and computational evaluation of carbazole-based bis-thiosemicarbazones: A selective enzyme inhibition study between ?-amylase and ?-glucosidase

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dc.authorid0000-0002-8325-8116en_US
dc.authorid0000-0003-0744-0968en_US
dc.authorid0000-0001-9386-4892en_US
dc.authorid0000-0002-3909-0694en_US
dc.contributor.authorŞahin, Hasan
dc.contributor.authorBingül, Alev Arslantürk
dc.contributor.authorŞengül, İbrahim Fazıl
dc.contributor.authorBingül, Murat
dc.date.accessioned2023-06-20T06:15:26Z
dc.date.available2023-06-20T06:15:26Z
dc.date.issued2023en_US
dc.departmentDicle Üniversitesi, Eczacılık Fakültesi, Eczacılık Meslek Bililmleri Bölümüen_US
dc.description.abstractBackground and Aims: Carbazole heterocyclic systems are an important class of chemicals that have been reported as valuable antidiabetic agents in the literature. Uncoincidentally, the ayurvedic antidiabetic plant Murraya koenigii Spreng (Curry tree) was the source of the first carbazole alkaloids. Another important class of chemicals in terms of antidiabetic activity is thiosemicarbazones. The hybridization of these fragments can create new potential inhibitors for α-amylase and α-glucosidase enzyme inhibitions, which is one approach controlling post-prandial hyperglycemia in type 2 diabetes patients. Methods: The four carbazole-based thiosemicarbazone compounds (4a-d) have been selected from the group library and α-amylase and α-glucosidase inhibition potencies have been evaluated. A molecular modelling study has also been carried out to provide a complementary study on how the molecules behave in terms of the enzymes’ catalytic properties. . Results: All compounds showed higher potencies than the standard acarbose in terms of α-glucosidase inhibition and very low inhibitions toward α-amylase compared to acarbose. Having the number of hydrophobic interactions determine the potency of the compounds was crucial with compound 4a being shown to provide the highest number of conventional H bonds and the highest percentage of inhibition values for both enzymes. Conclusion: Carbazole-based thiosemicarbazone compounds have been found to be promising candidates in terms of both their potency and relative selectivity for developing new inhibitors that lack the usual side effects of current drugs.en_US
dc.identifier.citationŞahin, H., Bingül, A. A., Şengül, İ. F. ve Bingül, M. (2023). Biological and computational evaluation of carbazole-based bis-thiosemicarbazones: A selective enzyme inhibition study between α-amylase and α-glucosidase. Istanbul Journal of Pharmacy, 53(1), 39-44.en_US
dc.identifier.doi10.26650/IstanbulJPharm.2023.1164443
dc.identifier.endpage44en_US
dc.identifier.issn2548-0731
dc.identifier.issn2587-2087
dc.identifier.issue1en_US
dc.identifier.startpage39en_US
dc.identifier.trdizinidTRDizinIdYok
dc.identifier.urihttps://search.trdizin.gov.tr/tr/yayin/detay/1176983
dc.identifier.urihttps://hdl.handle.net/11468/12090
dc.identifier.volume53en_US
dc.identifier.wosWOS:000995958300005
dc.identifier.wosqualityN/A
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakTR-Dizin
dc.institutionauthorŞahin, Hasan
dc.institutionauthorBingül, Alev Arslantürk
dc.institutionauthorBingül, Murat
dc.language.isoenen_US
dc.publisherIstanbul Universityen_US
dc.relation.ispartofIstanbul Journal of Pharmacy
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.titleBiological and computational evaluation of carbazole-based bis-thiosemicarbazones: A selective enzyme inhibition study between ?-amylase and ?-glucosidaseen_US
dc.titleBiological and computational evaluation of carbazole-based bis-thiosemicarbazones: A selective enzyme inhibition study between ?-amylase and ?-glucosidase
dc.typeArticleen_US

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