Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer

Abstract Aurein 1.2 is a potent antimicrobial peptide secreted by frog Litoria aurea. As a short membrane-active peptide with only 13 amino acids in sequence, it has been found to be residing on the surface of lipid bilayer and permeabilizing bacterial membranes at high concentration. However, the d...

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Autores principales:	Durgesh K. Rai, Shuo Qian
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d368b14970f24ee5adfae8eb066ea5e5
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spelling	oai:doaj.org-article:d368b14970f24ee5adfae8eb066ea5e52021-12-02T12:31:51ZInteraction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer10.1038/s41598-017-03795-62045-2322https://doaj.org/article/d368b14970f24ee5adfae8eb066ea5e52017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-03795-6https://doaj.org/toc/2045-2322Abstract Aurein 1.2 is a potent antimicrobial peptide secreted by frog Litoria aurea. As a short membrane-active peptide with only 13 amino acids in sequence, it has been found to be residing on the surface of lipid bilayer and permeabilizing bacterial membranes at high concentration. However, the detail at the molecular level is largely unknown. In this study, we investigated the action of Aurein 1.2 in charged lipid bilayers composed of DMPC/DMPG. Oriented Circular Dichroism results showed that the peptide was on the surface of lipid bilayer regardless of the charged lipid ratio. Only at a very high peptide-to-lipid ratio (~1/10), the peptide became perpendicular to the bilayer, however no pore was detected by neutron in-plane scattering. To further understand how it interacted with charged lipid bilayers, we employed Small Angle Neutron Scattering to probe lipid distribution across bilayer leaflets in lipid vesicles. The results showed that Aurein 1.2 interacted strongly with negatively charged DMPG, causing strong asymmetry in lipid bilayer. At high concentration, while the vesicles were intact, we found additional structure feature on the bilayer. Our study provides a glimpse into how Aurein 1.2 disturbs anionic lipid-containing membranes without pore formation.Durgesh K. RaiShuo QianNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Durgesh K. Rai Shuo Qian Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer
description	Abstract Aurein 1.2 is a potent antimicrobial peptide secreted by frog Litoria aurea. As a short membrane-active peptide with only 13 amino acids in sequence, it has been found to be residing on the surface of lipid bilayer and permeabilizing bacterial membranes at high concentration. However, the detail at the molecular level is largely unknown. In this study, we investigated the action of Aurein 1.2 in charged lipid bilayers composed of DMPC/DMPG. Oriented Circular Dichroism results showed that the peptide was on the surface of lipid bilayer regardless of the charged lipid ratio. Only at a very high peptide-to-lipid ratio (~1/10), the peptide became perpendicular to the bilayer, however no pore was detected by neutron in-plane scattering. To further understand how it interacted with charged lipid bilayers, we employed Small Angle Neutron Scattering to probe lipid distribution across bilayer leaflets in lipid vesicles. The results showed that Aurein 1.2 interacted strongly with negatively charged DMPG, causing strong asymmetry in lipid bilayer. At high concentration, while the vesicles were intact, we found additional structure feature on the bilayer. Our study provides a glimpse into how Aurein 1.2 disturbs anionic lipid-containing membranes without pore formation.
format	article
author	Durgesh K. Rai Shuo Qian
author_facet	Durgesh K. Rai Shuo Qian
author_sort	Durgesh K. Rai
title	Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer
title_short	Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer
title_full	Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer
title_fullStr	Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer
title_full_unstemmed	Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer
title_sort	interaction of the antimicrobial peptide aurein 1.2 and charged lipid bilayer
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d368b14970f24ee5adfae8eb066ea5e5
work_keys_str_mv	AT durgeshkrai interactionoftheantimicrobialpeptideaurein12andchargedlipidbilayer AT shuoqian interactionoftheantimicrobialpeptideaurein12andchargedlipidbilayer
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Interaction of the Antimicrobial Peptide Aurein 1.2 and Charged Lipid Bilayer

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