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Characterization of Hydroxyproline-Containing Hairpin-Like Antimicrobial Peptide EcAMP1-Hyp from Barnyard Grass (Echinochloa crusgalli L.) Seeds: Structural Identification and Comparative Analysis of Antifungal Activity

1
Department of Molecular Neurobiology, Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow 117997, Russia
2
Department of Chemical Studies with Biologically Active Compounds of Microbial Origin, Gause Institute of New Antibiotics, Moscow 119021, Russia
3
Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow 119991, Russia
4
Institute of Molecular Medicine, Sechenov First Moscow State Medical University, Moscow 119146, Russia
5
Department of Plant Protection, Timiryazev Russian State Agrarian University, Moscow 127550, Russia
*
Author to whom correspondence should be addressed.
Deceased on 4 January 2012.
Int. J. Mol. Sci. 2018, 19(11), 3449; https://doi.org/10.3390/ijms19113449
Received: 6 October 2018 / Revised: 29 October 2018 / Accepted: 30 October 2018 / Published: 2 November 2018
(This article belongs to the Section Bioactives and Nutraceuticals)
Herein, we describe a modified form of the antimicrobial hairpin-like peptide EcAMP1, isolated from barnyard grass (E. crusgalli) seeds, which is structurally characterized by a combination of high-pressure liquid chromatography, mass spectrometry, and automated Edman sequencing. This derivate has a single amino acid substitution (Pro19Hyp) in the second α-helical region of the molecule, which is critical for the formation of the hydrophobic core and the secondary structure elements. Comparing the antifungal activity of these two peptides, we found that the modified EcAMP1-Hyp had a significantly weaker activity towards the most-sensitive plant pathogenic fungus Fusarium solani. Molecular dynamics simulations and in vitro binding to the commercial polysaccharides allowed us to conclude that the Pro-19 residue is important for binding to carbohydrates located in the spore cell wall and it chiefly exhibits a fungistatic action representing the hyphal growth inhibition. These data are novel and significant for understanding a role of α-hairpinins in plant immunity. View Full-Text
Keywords: hairpin-like peptides; plant immunity; Echinochloa crusgalli; proline/hydroxyproline substitution; fungistatic activity; Fusarium solani; 3D modeling; in vitro binding assays hairpin-like peptides; plant immunity; Echinochloa crusgalli; proline/hydroxyproline substitution; fungistatic activity; Fusarium solani; 3D modeling; in vitro binding assays
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MDPI and ACS Style

Rogozhin, E.; Zalevsky, A.; Mikov, A.; Smirnov, A.; Egorov, T. Characterization of Hydroxyproline-Containing Hairpin-Like Antimicrobial Peptide EcAMP1-Hyp from Barnyard Grass (Echinochloa crusgalli L.) Seeds: Structural Identification and Comparative Analysis of Antifungal Activity. Int. J. Mol. Sci. 2018, 19, 3449. https://doi.org/10.3390/ijms19113449

AMA Style

Rogozhin E, Zalevsky A, Mikov A, Smirnov A, Egorov T. Characterization of Hydroxyproline-Containing Hairpin-Like Antimicrobial Peptide EcAMP1-Hyp from Barnyard Grass (Echinochloa crusgalli L.) Seeds: Structural Identification and Comparative Analysis of Antifungal Activity. International Journal of Molecular Sciences. 2018; 19(11):3449. https://doi.org/10.3390/ijms19113449

Chicago/Turabian Style

Rogozhin, Eugene, Artur Zalevsky, Alexander Mikov, Alexey Smirnov, and Tsezi Egorov. 2018. "Characterization of Hydroxyproline-Containing Hairpin-Like Antimicrobial Peptide EcAMP1-Hyp from Barnyard Grass (Echinochloa crusgalli L.) Seeds: Structural Identification and Comparative Analysis of Antifungal Activity" International Journal of Molecular Sciences 19, no. 11: 3449. https://doi.org/10.3390/ijms19113449

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