Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/50532
Full metadata record
DC FieldValueLanguage
dc.contributor.authorThinzar Win.
dc.date.accessioned2012-06-11T08:53:37Z
dc.date.available2012-06-11T08:53:37Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.urihttp://hdl.handle.net/10356/50532
dc.description.abstractFerritin is engineered as a targeted carrier for therapeutic and diagnostic agents. It is a naturally occurring biomaterial and functions in iron homeostasis in various organisms. The ferritin in this study is a protein cage derived from an archaeon Archaeoglobus fulgidus with unique self-assembling properties and remarkable heat stability. Due to its proteinaceous nature, the A. fulgidus ferritin (AfFtn) contains readily available reactive moiety for functionalization with targeting ligands. In this study, we have coupled mutant A. fulgidus ferritin (AfFtn-AA) with single-chain variable fragment (scFv) antibody to the surface of the protein cage for targeting purpose.en_US
dc.format.extent48 p.en_US
dc.language.isoenen_US
dc.subjectDRNTU::Engineering::Chemical engineeringen_US
dc.titleConjugation of antibody fragments to ferritin protein cage for targeted delivery to cancer cells.en_US
dc.typeThesis
dc.contributor.supervisorLim Sierinen_US
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.description.degree​Master of Science (Biomedical Engineering)en_US
item.fulltextWith Fulltext-
item.grantfulltextrestricted-
Appears in Collections:SCBE Theses
Files in This Item:
File Description SizeFormat 
ThinzarWin2012.pdf
  Restricted Access
1.11 MBAdobe PDFView/Open

Page view(s) 20

456
Updated on Dec 3, 2020

Download(s) 50

20
Updated on Dec 3, 2020

Google ScholarTM

Check

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.