Disulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli)
| Autor: | Yuri V. Baranov, Olga V. Samsonova, T. A. Balashova, Eugene A. Rogozhin, Alexander S. Arseniev, Alexey V. Feofanov, Nikolay A. Barinov, Alexander A. Vassilevski, Tsezi A. Egorov, Svetlana B. Nolde, Eugene V. Grishin |
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| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Antifungal Agents biology Trypsin inhibitor Antimicrobial peptides Fungi Peptide Cell Biology Echinochloa biology.organism_classification Biochemistry Echinochloa crus-galli Protein Structure Secondary Protein structure chemistry Protein Structure and Folding Protein purification Peptides Structural motif Molecular Biology Plant Diseases Plant Proteins |
| Zdroj: | Journal of Biological Chemistry. 286:25145-25153 |
| ISSN: | 0021-9258 |
| Popis: | This study presents purification, activity characterization, and (1)H NMR study of the novel antifungal peptide EcAMP1 from kernels of barnyard grass Echinochloa crus-galli. The peptide adopts a disulfide-stabilized α-helical hairpin structure in aqueous solution and thus represents a novel fold among naturally occurring antimicrobial peptides. Micromolar concentrations of EcAMP1 were shown to inhibit growth of several fungal phytopathogens. Confocal microscopy revealed intensive EcAMP1 binding to the surface of fungal conidia followed by internalization and accumulation in the cytoplasm without disturbance of membrane integrity. Close spatial structure similarity between EcAMP1, the trypsin inhibitor VhTI from seeds of Veronica hederifolia, and some scorpion and cone snail toxins suggests natural elaboration of different functions on a common fold. |
| Databáze: | OpenAIRE |
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