Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/39916
Title: Construction and characterisation of a siclopps cyclic peptide library.
Authors: Koh, Ethel Rui Li.
Keywords: DRNTU::Science::Biological sciences::Biochemistry
Issue Date: 2010
Abstract: Cyclic peptide libraries are valuable as they are significantly resistant to cellular catabolism, making them useful for manipulation of cellular processes, and their conformational stability allows greater potency in binding to target receptors. SICLOPPs (Split-Intein Circular Ligation of Peptides and Proteins), developed from the engineering of natural protein splicing machinery, is a powerful and versatile tool for the generation of cyclic peptide in vivo. In addition, libraries based on this technology are genetically encoded thereby providing large diversities, simple generation, and endogenous tagging which are all advantageous over synthetically generated peptide libraries. This project employs PCR based cloning to encode a novel SICLOPPs cyclic peptide library which has a potential diversity of 1.4 x 107 members and when characterised was found to have 40% efficiency. This work highlights the ease and many benefits of using genetic protein splicing techniques to create cyclic peptide libraries of high diversities that can be readily screened for in vivo applications.
URI: http://hdl.handle.net/10356/39916
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Student Reports (FYP/IA/PA/PI)

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