Construction and characterisation of a siclopps cyclic peptide library.

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...

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Main Author: Koh, Ethel Rui Li.
Other Authors: School of Physical and Mathematical Sciences
Format: Final Year Project (FYP)
Language:English
Published: 2010
Subjects:
Online Access:http://hdl.handle.net/10356/39916
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author Koh, Ethel Rui Li.
author2 School of Physical and Mathematical Sciences
author_facet School of Physical and Mathematical Sciences
Koh, Ethel Rui Li.
author_sort Koh, Ethel Rui Li.
collection NTU
description 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.
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spelling ntu-10356/399162023-02-28T23:10:46Z Construction and characterisation of a siclopps cyclic peptide library. Koh, Ethel Rui Li. School of Physical and Mathematical Sciences Brendan Patrick Orner DRNTU::Science::Biological sciences::Biochemistry 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. Bachelor of Science in Chemistry and Biological Chemistry 2010-06-08T02:02:03Z 2010-06-08T02:02:03Z 2010 2010 Final Year Project (FYP) http://hdl.handle.net/10356/39916 en 40 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences::Biochemistry
Koh, Ethel Rui Li.
Construction and characterisation of a siclopps cyclic peptide library.
title Construction and characterisation of a siclopps cyclic peptide library.
title_full Construction and characterisation of a siclopps cyclic peptide library.
title_fullStr Construction and characterisation of a siclopps cyclic peptide library.
title_full_unstemmed Construction and characterisation of a siclopps cyclic peptide library.
title_short Construction and characterisation of a siclopps cyclic peptide library.
title_sort construction and characterisation of a siclopps cyclic peptide library
topic DRNTU::Science::Biological sciences::Biochemistry
url http://hdl.handle.net/10356/39916
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