Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/23159
Title: Design of novel bioactive peptides using conotoxin scaffold
Authors: KANG TSE SIANG
Keywords: conotoxin, peptide, folding, NMR, scaffold
Issue Date: 28-Jun-2007
Source: KANG TSE SIANG (2007-06-28). Design of novel bioactive peptides using conotoxin scaffold. ScholarBank@NUS Repository.
Abstract: I?-conotoxins and I?/I>-conotoxins are short peptides with the same four conserved cysteines, but with distinct disulfide pairing (C1-3, C2-4 and C1-3, C2-4 respectively) resulting in globular and ribbon conformations. Through sequence alignment and subsequent studies using synthetic analogues, we have identified the importance of proline in the first intercysteine loop and C-terminal amide for the differential folding of these peptides. The folding propensities, as determined by coelution with regiospecifically synthesized conformers and NMR spectroscopy, indicate that these structural features act as conformations switches. Consequent conformation changes substantially impact the binding affinity of ImI conotoxin analogues to Aplysia Acetylcholine binding protein. The compact framework of these conotoxins present as attractive mini-protein scaffolds for presenting bioactive segments. As such, we have introduced RGD and KTS tripeptide sequences to design inhibitors of I?IIbI?3 and I?1I?1 integrin receptors in this scaffold.
URI: http://scholarbank.nus.edu.sg/handle/10635/23159
Appears in Collections:Ph.D Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
Title page.pdf179.83 kBAdobe PDF

OPEN

NoneView/Download
Preface.pdf107.68 kBAdobe PDF

OPEN

NoneView/Download
Chapter 1.pdf1.22 MBAdobe PDF

OPEN

NoneView/Download
Chapter 2.pdf597.3 kBAdobe PDF

OPEN

NoneView/Download
Chapter 3.pdf2.75 MBAdobe PDF

OPEN

NoneView/Download
Chapter 4.pdf451.4 kBAdobe PDF

OPEN

NoneView/Download
Chapter 5.pdf689.12 kBAdobe PDF

OPEN

NoneView/Download
Chapter 6.pdf178.68 kBAdobe PDF

OPEN

NoneView/Download

Page view(s)

231
checked on Dec 11, 2017

Download(s)

1,093
checked on Dec 11, 2017

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.