Peripheral Antimicrobial Peptide Gomesin Induces Membrane Protrusion, Folding, and Laceration

Optical microscopy shows that the peripheral antimicrobial peptide (AMP) gomesin does not disrupt the bacterial membrane by forming stable transmembrane pores but induces lipid accumulation domains, which is followed by a sudden burst near the domains. The molecular action mechanisms of gomesin on v...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 35(2019), 40 vom: 08. Okt., Seite 13233-13242
1. Verfasser: Zhang, Shan (VerfasserIn)
Weitere Verfasser: Fu, Lei, Wan, Mingwei, Song, Junjie, Gao, Lianghui, Fang, Weihai
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Anti-Bacterial Agents Antimicrobial Cationic Peptides Lipid Bilayers Liposomes gomesin Melitten 20449-79-0
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520 |a Optical microscopy shows that the peripheral antimicrobial peptide (AMP) gomesin does not disrupt the bacterial membrane by forming stable transmembrane pores but induces lipid accumulation domains, which is followed by a sudden burst near the domains. The molecular action mechanisms of gomesin on vesicle and planar bilayer membranes are investigated in this work using coarse-grained molecular dynamics simulations. By comparing the membrane morphology and property changes induced by gomesin and the pore-forming AMP melittin, we determined that the amphiphilic shape of the AMPs is a key factor affecting the mechanism of cell death. The binding of wedge-shaped gomesin, with a small hydrophobic surface, onto the membrane induces protrusion and folding of the outer monolayer followed by sudden membrane lacerations at the axillae of the protuberances. Alternatively, cylinder-shaped melittins with comparable hydrophilic and hydrophobic surfaces destroy membranes by forming stable pores coexisting with exocytosis-like buddings and endocytosis-like invaginations. The multiple actions of AMPs on the bacterial membrane suggest diverse paradigms for designing molecular carriers for delivering drugs to the cell 
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700 1 |a Fu, Lei  |e verfasserin  |4 aut 
700 1 |a Wan, Mingwei  |e verfasserin  |4 aut 
700 1 |a Song, Junjie  |e verfasserin  |4 aut 
700 1 |a Gao, Lianghui  |e verfasserin  |4 aut 
700 1 |a Fang, Weihai  |e verfasserin  |4 aut 
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