Please use this identifier to cite or link to this item:
Title: Design and characterization of functional novel oligopeptides
Keywords: Alternating ionic sequences, peptides, biomineralization, self-assembly
Issue Date: 6-Apr-2004
Citation: ONG BOON TEE (2004-04-06). Design and characterization of functional novel oligopeptides. ScholarBank@NUS Repository.
Abstract: The present study focus on the design, synthesis and functional role of a few oligopeptides. Towards this, we designed four peptides with primary sequence of alternating hydrophobic and hydrophilic amino acid residues incorporating calcium binding functional groups and motifs. As a preliminary step towards the development of peptide-based materials, we studied the self-assembly of these peptides under various conditions. In addition to these, the peptides were used as model system for understanding the protein-mineral interaction in biomineralization. Among the four peptides synthesized, two of them (P3 and P4) gave fiber-like structures on mica substrate, whereas spherical particles were observed for the peptides (P1 and P2). In the mineralization studies, all four peptides did not show significant effect on aggregation or polymorph selectivity in the calcium carbonate crystallization.
Appears in Collections:Master's Theses (Open)

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
OngBT.pdf1.74 MBAdobe PDF



Page view(s)

checked on May 23, 2019


checked on May 23, 2019

Google ScholarTM


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