Publication:
In vitro interaction of glutathione S‐transferase‐pi enzyme with glutathione‐coated silver sulfide quantum dots: a novel method for biodetection of glutathione S‐transferase enzyme

dc.contributor.departmentN/A
dc.contributor.departmentN/A
dc.contributor.departmentDepartment of Chemistry
dc.contributor.departmentN/A
dc.contributor.kuauthorAydemir, Duygu
dc.contributor.kuauthorHashemkhani, Mahshid
dc.contributor.kuauthorAcar, Havva Funda Yağcı
dc.contributor.kuauthorUlusu, Nuriye Nuray
dc.contributor.kuprofilePhD Student
dc.contributor.kuprofilePhD Student
dc.contributor.kuprofileFaculty Member
dc.contributor.kuprofileFaculty Member
dc.contributor.otherDepartment of Chemistry
dc.contributor.researchcenterKoç University Research Center for Translational Medicine (KUTTAM) / Koç Üniversitesi Translasyonel Tıp Araştırma Merkezi (KUTTAM)
dc.contributor.researchcenterKoç University Surface Science and Technology Center (KUYTAM) / Koç Üniversitesi Yüzey Teknolojileri Araştırmaları Merkezi (KUYTAM)
dc.contributor.schoolcollegeinstituteGraduate School of Health Sciences
dc.contributor.schoolcollegeinstituteGraduate School of Sciences and Engineering
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteSchool of Medicine
dc.contributor.yokidN/A
dc.contributor.yokidN/A
dc.contributor.yokid178902
dc.contributor.yokid6807
dc.date.accessioned2024-11-09T23:34:40Z
dc.date.issued2019
dc.description.abstractQuantum dots (QD) are being evaluated as inorganic nanoparticles for both in vitro and in vivo optical imaging. They are also used as sensors or vehicles for targeted drug delivery combined with optical imaging. In this study, we demonstrated that glutathione-coated Ag2S QDs (GSH-Ag2S QDs) act as a substrate analogue of glutathione S-transferase (GST) enzymes for the first time in the literature. The GSTs belong to a major group of detoxification enzymes involved in the detoxification metabolism responsible for the protection of cells against reactive oxygen species (ROS) or electrophiles. GST isozymes are impaired in the various diseases such as neurological diseases and cancer. We evaluated the interaction of GST-pi enzyme with GSH-Ag2S QDs, which have never been studied in the literature before, using both fluorometric and spectrophotometric methods. Our data showed that GSH-Ag2S QDs gave reaction with GST enzyme as a substrate analogue. In conclusion, our data may help to guide researchers for further development of sensing systems for GST activity which is impaired in various diseases including cancer.
dc.description.indexedbyWoS
dc.description.indexedbyScopus
dc.description.indexedbyPubMed
dc.description.issue6
dc.description.openaccessNO
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuN/A
dc.description.volume94
dc.identifier.doi10.1111/cbdd.13614
dc.identifier.eissn1747-0285
dc.identifier.issn1747-0277
dc.identifier.quartileQ3
dc.identifier.scopus2-s2.0-85071891318
dc.identifier.urihttp://dx.doi.org/10.1111/cbdd.13614
dc.identifier.urihttps://hdl.handle.net/20.500.14288/12369
dc.identifier.wos485454500001
dc.keywordsBiodetection
dc.keywordsCDNB
dc.keywordsGSH
dc.keywordsGSH‐Ag2S QDs
dc.keywordsGST
dc.languageEnglish
dc.publisherWiley
dc.sourceChemical Biology and Drug Design
dc.subjectBiochemistry and molecular biology
dc.subjectChemistry, medicinal
dc.titleIn vitro interaction of glutathione S‐transferase‐pi enzyme with glutathione‐coated silver sulfide quantum dots: a novel method for biodetection of glutathione S‐transferase enzyme
dc.typeJournal Article
dspace.entity.typePublication
local.contributor.authorid0000-0002-6449-2708
local.contributor.authorid0000-0002-8436-2214
local.contributor.authorid0000-0001-5601-8814
local.contributor.authorid0000-0002-3173-1389
local.contributor.kuauthorAydemir, Duygu
local.contributor.kuauthorHashemkhani, Mahshid
local.contributor.kuauthorAcar, Havva Funda Yağcı
local.contributor.kuauthorUlusu, Nuriye Nuray
relation.isOrgUnitOfPublication035d8150-86c9-4107-af16-a6f0a4d538eb
relation.isOrgUnitOfPublication.latestForDiscovery035d8150-86c9-4107-af16-a6f0a4d538eb

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