Antifungal Peptide Modeling, Folding and Mimetic Design

The antifungal peptides represent diverse structures for drug design. Unfortunately, they provide inferior drug candidates because of their low oral bioavailability, potential immunogenicity, poor in vivo metabolic stability and high molecular weight. Recent efforts have focused on the creation o...

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Main Author:	Moradi, Shoeib
Format:	Thesis
Language:	English English
Published:	2009
Subjects:	Peptides Antifungal agents
Online Access:	http://psasir.upm.edu.my/id/eprint/9822/1/FBSB_2009_30_A.pdf
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id	my-upm-ir.9822
record_format	uketd_dc
spelling	my-upm-ir.98222013-05-27T07:43:51Z Antifungal Peptide Modeling, Folding and Mimetic Design 2009-10 Moradi, Shoeib The antifungal peptides represent diverse structures for drug design. Unfortunately, they provide inferior drug candidates because of their low oral bioavailability, potential immunogenicity, poor in vivo metabolic stability and high molecular weight. Recent efforts have focused on the creation of non-natural peptide mimetics. Their artificial backbone makes most peptidomimetics resistant to degradative enzymes, thus, increasing the stability of peptidomimetic drugs in the body. In the present study, four antifungal peptidomimetics structures named C1 to C4 were designed based on the antifungal decapeptide crystallized structure of Pep-1 using bioinformatics tools. Structures C1 and C2 belong to the N-terminal part of Pep-1 and C3 and C4 belong to the C-terminal amino acid sequence part of Pep-1. Minimum inhibitory concentrations (MIC) of these structures were estimated against Aspergillus niger N402, Candida albicans ATCC 10231, and Saccharomyces cerevisiae PTCC 5052. Structures C2 and C1 showed more potent antifungal activities against these fungal strains compared to C3 and C4, respectively. This demonstrated that the N-terminal part is more potent for antifungal activity and indicated that the N-terminal part of antifungal peptides is more active and important for antifungal activity than the C-terminal. Structure C2 was demonstrated to be more active against these microorganisms and could be used as a potential target for future antifungal peptidomimetics studies. Important factors/descriptors of 63 antifungal peptides have been studied using Artificial Neural Network (ANN). The most important factors determined were amino acid number 1 (S1), Log P, and their α-helix contents. This is the first study on the structure of C1 to C4 peptidomimetics on Aspergillus niger N402, Candida albicans ATCC 10231, and Saccharomyces cerevisiae PTCC 5052. Peptides Antifungal agents 2009-10 Thesis http://psasir.upm.edu.my/id/eprint/9822/ http://psasir.upm.edu.my/id/eprint/9822/1/FBSB_2009_30_A.pdf application/pdf en public masters Universiti Putra Malaysia Peptides Antifungal agents Faculty Biotechnology and Biomolecular Sciences English
institution	Universiti Putra Malaysia
collection	PSAS Institutional Repository
language	English English
topic	Peptides Antifungal agents
spellingShingle	Peptides Antifungal agents Moradi, Shoeib Antifungal Peptide Modeling, Folding and Mimetic Design
description	The antifungal peptides represent diverse structures for drug design. Unfortunately, they provide inferior drug candidates because of their low oral bioavailability, potential immunogenicity, poor in vivo metabolic stability and high molecular weight. Recent efforts have focused on the creation of non-natural peptide mimetics. Their artificial backbone makes most peptidomimetics resistant to degradative enzymes, thus, increasing the stability of peptidomimetic drugs in the body. In the present study, four antifungal peptidomimetics structures named C1 to C4 were designed based on the antifungal decapeptide crystallized structure of Pep-1 using bioinformatics tools. Structures C1 and C2 belong to the N-terminal part of Pep-1 and C3 and C4 belong to the C-terminal amino acid sequence part of Pep-1. Minimum inhibitory concentrations (MIC) of these structures were estimated against Aspergillus niger N402, Candida albicans ATCC 10231, and Saccharomyces cerevisiae PTCC 5052. Structures C2 and C1 showed more potent antifungal activities against these fungal strains compared to C3 and C4, respectively. This demonstrated that the N-terminal part is more potent for antifungal activity and indicated that the N-terminal part of antifungal peptides is more active and important for antifungal activity than the C-terminal. Structure C2 was demonstrated to be more active against these microorganisms and could be used as a potential target for future antifungal peptidomimetics studies. Important factors/descriptors of 63 antifungal peptides have been studied using Artificial Neural Network (ANN). The most important factors determined were amino acid number 1 (S1), Log P, and their α-helix contents. This is the first study on the structure of C1 to C4 peptidomimetics on Aspergillus niger N402, Candida albicans ATCC 10231, and Saccharomyces cerevisiae PTCC 5052.
format	Thesis
qualification_level	Master's degree
author	Moradi, Shoeib
author_facet	Moradi, Shoeib
author_sort	Moradi, Shoeib
title	Antifungal Peptide Modeling, Folding and Mimetic Design
title_short	Antifungal Peptide Modeling, Folding and Mimetic Design
title_full	Antifungal Peptide Modeling, Folding and Mimetic Design
title_fullStr	Antifungal Peptide Modeling, Folding and Mimetic Design
title_full_unstemmed	Antifungal Peptide Modeling, Folding and Mimetic Design
title_sort	antifungal peptide modeling, folding and mimetic design
granting_institution	Universiti Putra Malaysia
granting_department	Faculty Biotechnology and Biomolecular Sciences
publishDate	2009
url	http://psasir.upm.edu.my/id/eprint/9822/1/FBSB_2009_30_A.pdf
_version_	1747811003040530432

Antifungal Peptide Modeling, Folding and Mimetic Design

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