<abstract xmlns="http://www.w3.org/1999/xhtml"><p>Antimicrobial peptides (AMPs) are cationic small peptide chains that have good antimicrobial activity against a variety of bacteria, fungi, and viruses. AMP-17 is a recombinant insect AMP obtained by a prokaryotic expression system. However, the full antifungal activity, physicochemical characteristics, and cytotoxicity of AMP-17 were previously unknown. AMP-17 was shown to have good antifungal activity against five pathogenic fungi, with minimum inhibitory concentrations (MIC) of 9.375–18.75 μg/ml, and minimum fungicidal concentrations (MFC) of 18.75–37.5 μg/ml. Notably, the antifungal activity of AMP-17 against <italic>Cryptococcus neoformans</italic> was superior to that of other <italic>Candida</italic> spp. In addition, the hemolytic rate of AMP-17 was only 1.47%, even at the high concentration of 16× MIC. AMP-17 was insensitive to temperature and high salt ion concentration, with temperatures of 98°C and –80°C, and NaCl and MgCl<sub>2</sub> concentrations of 50–200 mmol/l, having no significant effect on antifungal activity. However, AMP-17 was sensitive to proteases, trypsin, pepsin, and proteinase K. The elucidation of antifungal activity, physicochemical properties and cytotoxicity of AMP-17 provided an experimental basis for its safety evaluation and application, as well as indicated that AMP-17 might be a promising drug.</p></abstract>

Antimicrobial peptides (AMPs) are cationic small peptide chains that have good antimicrobial activity against a variety of bacteria, fungi, and viruses. AMP-17 is a recombinant insect AMP obtained by a prokaryotic expression system. However, the full antifungal activity, physicochemical characteristics, and cytotoxicity of AMP-17 were previously unknown. AMP-17 was shown to have good antifungal activity against five pathogenic fungi, with minimum inhibitory concentrations (MIC) of 9.375–18.75 μg/ml, and minimum fungicidal concentrations (MFC) of 18.75–37.5 μg/ml. Notably, the antifungal activity of AMP-17 against Cryptococcus neoformans was superior to that of other Candida spp. In addition, the hemolytic rate of AMP-17 was only 1.47%, even at the high concentration of 16× MIC. AMP-17 was insensitive to temperature and high salt ion concentration, with temperatures of 98°C and –80°C, and NaCl and MgCl2 concentrations of 50–200 mmol/l, having no significant effect on antifungal activity. However, AMP-17 was sensitive to proteases, trypsin, pepsin, and proteinase K. The elucidation of antifungal activity, physicochemical properties and cytotoxicity of AMP-17 provided an experimental basis for its safety evaluation and application, as well as indicated that AMP-17 might be a promising drug.

Antifungal Activity and Physicochemical Properties of a Novel Antimicrobial Protein AMP-17 from <italic>Musca domestica</italic>

Polish Journal of Microbiology

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Antifungal Activity and Physicochemical Properties of a Novel Antimicrobial Protein AMP-17 from 

Antimicrobial peptides (AMPs) are cationic small peptide chains that have good antimicrobial activity against a variety of bacteria, fungi, and viruses. AMP-17...

Antifungal Activity and Physicochemical Properties of a Novel Antimicrobial Protein AMP-17 from Musca domestica

Article Category: original-paper

Publicado en línea: 03 sept 2019

Páginas: 383 - 390

Recibido: 15 jun 2019

Aceptado: 04 ago 2019

DOI: https://doi.org/10.33073/pjm-2019-041

Palabras clave
antimicrobial peptides, AMP-17, antifungal activity, stability, hemolytic activity

© 2019 Anton Pyskun et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Antifungal Activity and Physicochemical Properties of a Novel Antimicrobial Protein AMP-17 from Musca domestica

Article Category: original-paper

Publicado en línea: 03 sept 2019

Páginas: 383 - 390

Recibido: 15 jun 2019

Aceptado: 04 ago 2019

DOI: https://doi.org/10.33073/pjm-2019-041

Palabras claveantimicrobial peptides, AMP-17, antifungal activity, stability, hemolytic activity

© 2019 Anton Pyskun et al., published by Sciendo

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Palabras clave
antimicrobial peptides, AMP-17, antifungal activity, stability, hemolytic activity