Bioavailability and biocompatibility of tetrabranched antifungal peptides.

Fungal keratitis is the second leading cause of corneal blindness in the developing countries. Fungal resistance becomes a serious threat in maintaining public health due to the recurrent use of antibiotic therapy. Thus, new therapeutic approach is essential to replace the conventional antibiotics....

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Main Author: Lim, Yih Lin.
Other Authors: School of Biological Sciences
Format: Final Year Project
Language:English
Published: 2012
Subjects:
Online Access:http://hdl.handle.net/10356/49393
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-493932023-02-28T18:01:31Z Bioavailability and biocompatibility of tetrabranched antifungal peptides. Lim, Yih Lin. School of Biological Sciences Singapore Eye Research Institute Roger Beuerman R Lakshminarayanan DRNTU::Science::Biological sciences::Biochemistry Fungal keratitis is the second leading cause of corneal blindness in the developing countries. Fungal resistance becomes a serious threat in maintaining public health due to the recurrent use of antibiotic therapy. Thus, new therapeutic approach is essential to replace the conventional antibiotics. B4010, a tetrabranched antifungal peptide is developed by Prof. Roger Beuerman’s group at SERI. The aim of this study is to assess the therapeutic potential of B4010 and its four truncated analogues and the scrambled peptide for topical and systemic fungal infections. The antifungal properties of these peptides were tested against 3 C. albicans and their antifungal activities were determined in presence of trypsin (1:100 enzyme: substrate ratio), 25% human serum and 50% tear fluid in vitro. Furthermore, we determined the dissipation of cytoplasmic membrane potential upon adding various peptides to C. albicans ATCC 10231 as well as the haemolytic activity of the peptides in rabbit blood. B4010∆1-5 has evidently shown to be the most effective peptide with low MIC of 12uM and considerably stable in the presence of trypsin, human serum and tear fluid, and exhibit good fungicidal action but strong haemolytic activity. This concludes B4010∆1-5 is the ideal B4010 truncated derivative for further drug-optimization process. Bachelor of Science in Biological Sciences 2012-05-18T03:20:21Z 2012-05-18T03:20:21Z 2012 2012 Final Year Project (FYP) http://hdl.handle.net/10356/49393 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::Biological sciences::Biochemistry
spellingShingle DRNTU::Science::Biological sciences::Biochemistry
Lim, Yih Lin.
Bioavailability and biocompatibility of tetrabranched antifungal peptides.
description Fungal keratitis is the second leading cause of corneal blindness in the developing countries. Fungal resistance becomes a serious threat in maintaining public health due to the recurrent use of antibiotic therapy. Thus, new therapeutic approach is essential to replace the conventional antibiotics. B4010, a tetrabranched antifungal peptide is developed by Prof. Roger Beuerman’s group at SERI. The aim of this study is to assess the therapeutic potential of B4010 and its four truncated analogues and the scrambled peptide for topical and systemic fungal infections. The antifungal properties of these peptides were tested against 3 C. albicans and their antifungal activities were determined in presence of trypsin (1:100 enzyme: substrate ratio), 25% human serum and 50% tear fluid in vitro. Furthermore, we determined the dissipation of cytoplasmic membrane potential upon adding various peptides to C. albicans ATCC 10231 as well as the haemolytic activity of the peptides in rabbit blood. B4010∆1-5 has evidently shown to be the most effective peptide with low MIC of 12uM and considerably stable in the presence of trypsin, human serum and tear fluid, and exhibit good fungicidal action but strong haemolytic activity. This concludes B4010∆1-5 is the ideal B4010 truncated derivative for further drug-optimization process.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Lim, Yih Lin.
format Final Year Project
author Lim, Yih Lin.
author_sort Lim, Yih Lin.
title Bioavailability and biocompatibility of tetrabranched antifungal peptides.
title_short Bioavailability and biocompatibility of tetrabranched antifungal peptides.
title_full Bioavailability and biocompatibility of tetrabranched antifungal peptides.
title_fullStr Bioavailability and biocompatibility of tetrabranched antifungal peptides.
title_full_unstemmed Bioavailability and biocompatibility of tetrabranched antifungal peptides.
title_sort bioavailability and biocompatibility of tetrabranched antifungal peptides.
publishDate 2012
url http://hdl.handle.net/10356/49393
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