Publication:
Structure based drug design for insulin degrading enzyme (IDE)

dc.contributor.departmentDepartment of Chemical and Biological Engineering
dc.contributor.departmentDepartment of Industrial Engineering
dc.contributor.departmentGraduate School of Sciences and Engineering
dc.contributor.kuauthorÇakır, Bilal
dc.contributor.kuauthorDağlıyan, Onur
dc.contributor.kuauthorDağyıldız, Ezgi
dc.contributor.kuauthorKavaklı, İbrahim Halil
dc.contributor.kuauthorKızılel, Seda
dc.contributor.kuauthorTürkay, Metin
dc.contributor.schoolcollegeinstituteCollege of Engineering
dc.contributor.schoolcollegeinstituteGRADUATE SCHOOL OF SCIENCES AND ENGINEERING
dc.date.accessioned2024-11-10T00:02:56Z
dc.date.issued2010
dc.description.abstractInsulin-degrading enzyme (IDE) is an allosteric Zn +2 metalloprotease involved in the degradation of many peptides including amyloid beta (Aβ), and insulin that play key roles in Alzheimer's disease (AD) and type 2 diabetes mellitus (T2DM), respectively. Crystal structure of IDE revealed that N-terminal of IDE has an exosite which serves as a regulation site by orientation of the substrates of IDE to the catalytic site. It is plausible to find small molecules that bind to the exosite of IDE and enhance its proteolytic activity towards different substrates. In this study, we have taken a computer-aided structure based drug design methods combined with experimental methods, one novel molecule that enhances the activity of human IDE was discovered. The novel compound, designated as D10 enhanced both IDE mediated proteolysis of substrate V and insulin degradation. This study describes the first examples of a computer-aided discovery of IDE regulators, showing that in vitro activation of this important enzyme with drug-like small molecules is attainable.
dc.description.indexedbyScopus
dc.description.openaccessYES
dc.description.publisherscopeInternational
dc.description.sponsoredbyTubitakEuN/A
dc.identifier.isbn9780-8169-1065-6
dc.identifier.linkhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-78751478248andpartnerID=40andmd5=9f7954f5a1f7b03ce8acdc492df674b0
dc.identifier.quartileN/A
dc.identifier.urihttps://hdl.handle.net/20.500.14288/16238
dc.keywordsAlzheimer's disease
dc.keywordsAmyloid betas
dc.keywordsCatalytic sites
dc.keywordsDifferent substrates
dc.keywordsExperimental methods
dc.keywordsIn-vitro
dc.keywordsInsulin degradation
dc.keywordsInsulin-degrading enzymes
dc.keywordsMetallo-protease
dc.keywordsN-terminals
dc.keywordsNovel molecules
dc.keywordsProteolytic activities
dc.keywordsSmall molecules
dc.keywordsStructure based drug designs
dc.keywordsType 2 diabetes mellitus
dc.keywordsCrystal orientation
dc.keywordsDegradation
dc.keywordsEnzymes
dc.keywordsInsulin
dc.keywordsMolecules
dc.keywordsSubstrates
dc.keywordsIntegrodifferential equations
dc.language.isoeng
dc.publisherAICHE
dc.relation.ispartofAIChE Annual Meeting, Conference Proceedings
dc.subjectIndustrial engineering
dc.titleStructure based drug design for insulin degrading enzyme (IDE)
dc.typeConference Proceeding
dspace.entity.typePublication
local.contributor.kuauthorTürkay, Metin
local.contributor.kuauthorKızılel, Seda
local.contributor.kuauthorKavaklı, İbrahim Halil
local.contributor.kuauthorDağlıyan, Onur
local.contributor.kuauthorDağyıldız, Ezgi
local.contributor.kuauthorÇakır, Bilal
local.publication.orgunit1College of Engineering
local.publication.orgunit1GRADUATE SCHOOL OF SCIENCES AND ENGINEERING
local.publication.orgunit2Department of Industrial Engineering
local.publication.orgunit2Department of Chemical and Biological Engineering
local.publication.orgunit2Graduate School of Sciences and Engineering
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