Antifungal Peptide Modeling, Folding and Mimetic Design: In silico approaches to design peptidomimetics

Antifungal Peptide Modeling, Folding and Mimetic Design: In silico approaches to design peptidomimetics


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von Shoeib Moradi

Beschreibung

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. Minimum inhibitory concentrations (MIC) of these structures were estimated against Aspergillus niger N402, Candida albicans ATCC 10231, and Saccharomyces cerevisiae PTCC 5052. It was demonstrated that the N-terminal part of antifungal peptides is more active and important for antifungal activity than the C-terminal. Also, important factors/descriptors of 63 antifungal peptides have been studied using Artificial Neural Network (ANN).


Tags: Biologie, Biochemie, Biophysik


Taschenbuch - 9783848428267
Verlag: LAP Lambert Academic Publishing
Ersterscheinung: April 2012
ISBN-13: 9783848428267
Größe: 220 mm x 151 mm x 12 mm
Gewicht: 186 Gramm
112 Seiten
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