Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.

Antimicrobial peptides are short defensive peptides that represent a promising therapeutic option to eradicate antimicrobial resistant strains that has long since been increasing in number. Temporin B is a natural antimicrobial peptide that has shown reduced efficacy on Gram-negative strains due to...

Full description

Saved in:
Bibliographic Details
Main Author: Goh, Su-Ann.
Other Authors: Surajit Bhattacharyya
Format: Final Year Project
Language:English
Published: 2013
Subjects:
Online Access:http://hdl.handle.net/10356/52495
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Nanyang Technological University
Language: English
id sg-ntu-dr.10356-52495
record_format dspace
spelling sg-ntu-dr.10356-524952023-02-28T18:05:34Z Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif. Goh, Su-Ann. Surajit Bhattacharyya School of Biological Sciences DRNTU::Science Antimicrobial peptides are short defensive peptides that represent a promising therapeutic option to eradicate antimicrobial resistant strains that has long since been increasing in number. Temporin B is a natural antimicrobial peptide that has shown reduced efficacy on Gram-negative strains due to its tendency to oligomerize on the lipopolysaccharide feature of the outer membrane. Conjugating Temporin B to a synthetic lipopolysaccharide binding motif termed β-boomerang domain, formed a synthetic peptide, LG21, with vastly improved antimicrobial activity. In this study, we attempt to understand the role of Temporin B component of LG21 by truncating the Temporin B portion, forming synthetic peptide LG14. LG14 was shown to have reduced antimicrobial activity but was still able to permeate the bacterial outer membrane and inner membrane, though comparatively less efficient in the latter. Fluorescence assays highlighted limited discrimination between eukaryotic membrane mimic and bacterial inner membrane mimic. Structural elucidation by circular dichroism and nuclear magnetic resonance spectroscopy of LG14 were in agreement on an α-helical conformation at bound state. NMR also indicated that the α-helix has little amphipathicity. Collectively, these results demonstrate that Temporin B played a role in conferring LG21 with antimicrobial activity especially in recognition and perturbation of the bacterial inner membrane. Bachelor of Science in Biological Sciences 2013-05-15T02:05:22Z 2013-05-15T02:05:22Z 2013 2013 Final Year Project (FYP) http://hdl.handle.net/10356/52495 en Nanyang Technological University 31 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science
spellingShingle DRNTU::Science
Goh, Su-Ann.
Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.
description Antimicrobial peptides are short defensive peptides that represent a promising therapeutic option to eradicate antimicrobial resistant strains that has long since been increasing in number. Temporin B is a natural antimicrobial peptide that has shown reduced efficacy on Gram-negative strains due to its tendency to oligomerize on the lipopolysaccharide feature of the outer membrane. Conjugating Temporin B to a synthetic lipopolysaccharide binding motif termed β-boomerang domain, formed a synthetic peptide, LG21, with vastly improved antimicrobial activity. In this study, we attempt to understand the role of Temporin B component of LG21 by truncating the Temporin B portion, forming synthetic peptide LG14. LG14 was shown to have reduced antimicrobial activity but was still able to permeate the bacterial outer membrane and inner membrane, though comparatively less efficient in the latter. Fluorescence assays highlighted limited discrimination between eukaryotic membrane mimic and bacterial inner membrane mimic. Structural elucidation by circular dichroism and nuclear magnetic resonance spectroscopy of LG14 were in agreement on an α-helical conformation at bound state. NMR also indicated that the α-helix has little amphipathicity. Collectively, these results demonstrate that Temporin B played a role in conferring LG21 with antimicrobial activity especially in recognition and perturbation of the bacterial inner membrane.
author2 Surajit Bhattacharyya
author_facet Surajit Bhattacharyya
Goh, Su-Ann.
format Final Year Project
author Goh, Su-Ann.
author_sort Goh, Su-Ann.
title Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.
title_short Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.
title_full Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.
title_fullStr Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.
title_full_unstemmed Resurrecting inactive antimicrobial peptide from LPS trap : activity, LPS-interactions and conformations of a hybrid peptide of temporin B and beta-boomerang motif.
title_sort resurrecting inactive antimicrobial peptide from lps trap : activity, lps-interactions and conformations of a hybrid peptide of temporin b and beta-boomerang motif.
publishDate 2013
url http://hdl.handle.net/10356/52495
_version_ 1759855948825886720