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Volume 56, Issue 5

An antifungal protein from No Access

Abstract

A cytosolic protein was purified from BL21 that demonstrated potent antifungal activity against pathogenic strains of ,, and . The MIC of purified protein from BL21 (PPEBL21) against species and was 1.95–3.98 and 15.62 μg ml, respectively. toxicity tests demonstrated no cytotoxicity of PPEBL21 to human erythrocytes up to the tested concentrations of 1250 μg ml. Amphotericin B was lethal to 100 % of human erythrocytes at a concentration of 37.5 μg ml. The N-terminal amino acid sequence of PPEBL21 was found to be DLAEVASR, which showed 75 % sequence similarity with alcohol dehydrogenase of yeast. Mass fingerprinting by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry also substantiated these observations. The results suggested that BL21 might be an important bioresource of lead molecules for developing new peptide-based therapies for treating fungal infections.

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Keyword(s): ADH, alcohol dehydrogenase and MALDI-TOF, matrix-assisted laser desorption/ionization time-of-flight
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2007-05-01
2026-01-22

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An antifungal protein from Escherichia coli
J. Med. Microbiol. 56, 637 (2007); https://doi.org/10.1099/jmm.0.46973-0
/content/journal/jmm/10.1099/jmm.0.46973-0
/content/journal/jmm/10.1099/jmm.0.46973-0
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