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Article

The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous Plant Drosera capensis

1
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA
2
Department of Chemistry, University of California, Irvine, CA 92697, USA
3
National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA
4
Departments of Sociology, Statistics, and Electrical Engineering and Computer Science, University of California, Irvine, CA 92697, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Biomolecules 2020, 10(7), 1069; https://doi.org/10.3390/biom10071069
Received: 14 June 2020 / Revised: 8 July 2020 / Accepted: 13 July 2020 / Published: 17 July 2020
(This article belongs to the Special Issue Advances in Membrane Proteins)
The Droserasins, aspartic proteases from the carnivorous plant Drosera capensis, contain a 100-residue plant-specific insert (PSI) that is post-translationally cleaved and independently acts as an antimicrobial peptide. PSIs are of interest not only for their inhibition of microbial growth, but also because they modify the size of lipid vesicles and strongly interact with biological membranes. PSIs may therefore be useful for modulating lipid systems in NMR studies of membrane proteins. Here we present the expression and biophysical characterization of the Droserasin 1 PSI (D1 PSI.) This peptide is monomeric in solution and maintains its primarily α -helical secondary structure over a wide range of temperatures and pH values, even under conditions where its three disulfide bonds are reduced. Vesicle fusion assays indicate that the D1 PSI strongly interacts with bacterial and fungal lipids at pH 5 and lower, consistent with the physiological pH of D. capensis mucilage. It binds lipids with a variety of head groups, highlighting its versatility as a potential stabilizer for lipid nanodiscs. Solid-state NMR spectra collected at a field strength of 36 T, using a unique series-connected hybrid magnet, indicate that the peptide is folded and strongly bound to the membrane. Molecular dynamics simulations indicate that the peptide is stable as either a monomer or a dimer in a lipid bilayer. Both the monomer and the dimer allow the passage of water through the membrane, albeit at different rates. View Full-Text
Keywords: antimicrobial peptide; membrane protein; lipid-protein interactions; solid-state NMR; Drosera capensis; carnivorous plant antimicrobial peptide; membrane protein; lipid-protein interactions; solid-state NMR; Drosera capensis; carnivorous plant
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MDPI and ACS Style

Sprague-Piercy, M.A.; Bierma, J.C.; Crosby, M.G.; Carpenter, B.P.; Takahashi, G.R.; Paulino, J.; Hung, I.; Zhang, R.; Kelly, J.E.; Kozlyuk, N.; Chen, X.; Butts, C.T.; Martin, R.W. The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous Plant Drosera capensis. Biomolecules 2020, 10, 1069. https://doi.org/10.3390/biom10071069

AMA Style

Sprague-Piercy MA, Bierma JC, Crosby MG, Carpenter BP, Takahashi GR, Paulino J, Hung I, Zhang R, Kelly JE, Kozlyuk N, Chen X, Butts CT, Martin RW. The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous Plant Drosera capensis. Biomolecules. 2020; 10(7):1069. https://doi.org/10.3390/biom10071069

Chicago/Turabian Style

Sprague-Piercy, Marc A., Jan C. Bierma, Marquise G. Crosby, Brooke P. Carpenter, Gemma R. Takahashi, Joana Paulino, Ivan Hung, Rongfu Zhang, John E. Kelly, Natalia Kozlyuk, Xi Chen, Carter T. Butts, and Rachel W. Martin 2020. "The Droserasin 1 PSI: A Membrane-Interacting Antimicrobial Peptide from the Carnivorous Plant Drosera capensis" Biomolecules 10, no. 7: 1069. https://doi.org/10.3390/biom10071069

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