Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 28, Pages 25145-25153Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.200378
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Funding
- Russian Foundation for Basic Research [08-04-00783, 11-04-00190]
- Ministry of Education and Science of Russian Federation [16.740.11.0424]
- Russian scientific schools [4821.2008.4]
- Russian Academy of Sciences
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This study presents purification, activity characterization, and H-1 NMR study of the novel antifungal peptide EcAMP1 from kernels of barnyard grass Echinochloa crus-galli. The peptide adopts a disulfide-stabilized alpha-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.
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