Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/52237
Full metadata record
DC FieldValueLanguage
dc.contributor.authorTao, Pengen
dc.date.accessioned2013-04-25T08:09:03Zen
dc.date.available2013-04-25T08:09:03Zen
dc.date.copyright2013en
dc.date.issued2013en
dc.identifier.citationTao, P. (2013). Understanding the self-assembly mechanism of E2 protein cage and exploring its potential applications. Doctoral thesis, Nanyang Technological University, Singapore.en
dc.identifier.urihttps://hdl.handle.net/10356/52237en
dc.description.abstractSelf-assembly protein cages have drawn much attention for their applications in nanotechnology. E2 protein from Bacillus stearothermophilus, which comprises 60 identical subunits to form hollow porous structure, has been demonstrated for being used as nanocapsule in drug delivery. To facilitate future applications such as controlled release, understanding the self-assembly mechanism of E2 protein is considered. We verify that self-assembly of E2 protein is mediated by protein C-terminus using trimer structure as intermediate. Based on understanding the role of inter-trimer interactions, we design pH-responsive E2 protein cages: i) by introducing histidine pairs, mutant protein maintains assembled at physiological pH while dissociates at acidic pH; ii) by substituting C-terminus with GALA peptide, mutant protein dissociates at neutral pH while assembles at acidic pH. To further explore functionalities of the E2 protein, iron-binding peptides are incorporated into the interior surface. The mutant E2 protein is capable of working as a size- and shape- constrained nano-reactor for iron biomineralization.en
dc.format.extent171 p.en
dc.language.isoenen
dc.subjectDRNTU::Engineering::Bioengineeringen
dc.titleUnderstanding the self-assembly mechanism of E2 protein cage and exploring its potential applicationsen
dc.typeThesisen
dc.contributor.supervisorLim Sierinen
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen
dc.description.degreeDOCTOR OF PHILOSOPHY (SCBE)en
dc.identifier.doi10.32657/10356/52237en
item.fulltextWith Fulltext-
item.grantfulltextopen-
Appears in Collections:SCBE Theses
Files in This Item:
File Description SizeFormat 
TscbeG0802543B.pdfFull Thesis3.32 MBAdobe PDFThumbnail
View/Open

Page view(s) 50

437
checked on Oct 23, 2020

Download(s) 50

174
checked on Oct 23, 2020

Google ScholarTM

Check

Altmetric


Plumx

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