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.departmentDepartment of Chemistry
dc.contributor.departmentGraduate School of Health Sciences
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.departmentKUTTAM (Koç University Research Center for Translational Medicine)
dc.contributor.departmentKUYTAM (Koç University Surface Science and Technology Center)
dc.contributor.departmentSchool of Medicine
dc.contributor.kuauthorAcar, Havva Funda Yağcı
dc.contributor.kuauthorAydemir, Duygu
dc.contributor.kuauthorHashemkhani, Mahshid
dc.contributor.kuauthorUlusu, Nuriye Nuray
dc.contributor.schoolcollegeinstituteCollege of Sciences
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF HEALTH SCIENCES
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.contributor.schoolcollegeinstituteResearch Center
dc.contributor.schoolcollegeinstituteSCHOOL OF MEDICINE
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.urihttps://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.language.isoeng
dc.publisherWiley
dc.relation.ispartofChemical 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.kuauthorAydemir, Duygu
local.contributor.kuauthorHashemkhani, Mahshid
local.contributor.kuauthorAcar, Havva Funda Yağcı
local.contributor.kuauthorUlusu, Nuriye Nuray
local.publication.orgunit1GRADUATE SCHOOL OF HEALTH SCIENCES
local.publication.orgunit1GRADUATE SCHOOL OF SCIENCES AND ENGINEERING
local.publication.orgunit1College of Sciences
local.publication.orgunit1SCHOOL OF MEDICINE
local.publication.orgunit1Research Center
local.publication.orgunit2Department of Chemistry
local.publication.orgunit2KUTTAM (Koç University Research Center for Translational Medicine)
local.publication.orgunit2KUYTAM (Koç University Surface Science and Technology Center)
local.publication.orgunit2School of Medicine
local.publication.orgunit2Graduate School of Health Sciences
local.publication.orgunit2Graduate School of Sciences and Engineering
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