Antifungal indole and pyrrolidine-2,4-Dione derivative peptidomimetic lead design based on in silico study of bioactive Peptide families. - RIIP - Réseau International des Instituts Pasteur Access content directly
Journal Articles Avicenna Journal of Medical Biotechnology Year : 2013

Antifungal indole and pyrrolidine-2,4-Dione derivative peptidomimetic lead design based on in silico study of bioactive Peptide families.

Abstract

BACKGROUND: The rise of opportunistic fungal infections highlights the need for development of new antimicrobial agents. Antimicrobial Peptides (AMPs) and Antifungal Peptides (AFPs) are among the agents with minimal resistance being developed against them, therefore they can be used as structural templates for design of new antimicrobial agents. METHODS: In the present study four antifungal peptidomimetic structures named C1 to C4 were designed based on plant defensin of Pisum sativum. Minimum inhibitory concentrations (MICs) for these structures were determined against Aspergillus niger N402, Candida albicans ATCC 10231, and Saccharomyces cerevisiae PTCC 5052. RESULTS: C1 and C2 showed more potent antifungal activity against these fungal strains compared to C3 and C4. The structure C2 demonstrated a potent antifungal activity among them and could be used as a template for future study on antifungal peptidomemetics design. Sequences alignments led to identifying antifungal decapeptide (KTCENLADTY) named KTC-Y, which its MIC was determined on fungal protoplast showing 25 (µg/ml) against Aspergillus fumigatus Af293. CONCLUSION: The present approach to reach the antifungal molecules seems to be a powerful approach in design of bioactive agents based on AMP mimetic identification.

Domains

Pharmacology
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Dates and versions

pasteur-00821604 , version 1 (11-05-2013)

Identifiers

  • HAL Id : pasteur-00821604 , version 1
  • PUBMED : 23626876

Cite

Shoeib Moradi, Parisa Azerang, Vahid Khalaj, Soroush Sardari. Antifungal indole and pyrrolidine-2,4-Dione derivative peptidomimetic lead design based on in silico study of bioactive Peptide families.. Avicenna Journal of Medical Biotechnology, 2013, 5 (1), pp.42-53. ⟨pasteur-00821604⟩

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