Characterization and lipid phase effect on the interaction of GBV-C E2-derived peptide, P6-2VIR576, with lipid membranes relating it with the HIV-1 FP inhibition

Highlights  Not everything has been said about the mechanism of action of melittin  Melittin has the ability to penetrate the zwitterionic lipid membranes under the right conditions  The existence of defects in a membrane favors the penetration of melittin  The penetration of melittin favors the increase of membrane defects ABSTRACT Melittin (ML) is a small peptide of 26 residues rich in arginine (Arg) and lysine (Lys). Several studies have been done to understand the mechanism of interaction with neutral and negatively charged lipids. However, it is not known with certainty how this interaction depends on the electrostatic or hydrophobic forces according to the composition of the membrane, nor with the different organization of lipids on the membrane, such as the microdomains that could take place in it. Therefore, comparative studies of the interaction and the effect of ML with respect to cationic peptides (Arg-7 and Lys-5) were conducted to get a deeper insight of the ML interaction mechanism with membranes. In this regard, measurements of zeta potential of different model membranes (DOPC, DMPC and DMPE liposomes) in the presence of the peptides, and molecular dynamics simulations were

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Filling gaps in the knowledge of melittin on lipid membranes

Tissera

Disalvo

Martini

et al. 2019

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Two/three-dimensional interfacial properties of the novel peptide as a selective destroyer of biomembrane

Wang

et al. 2019

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Lipid domains in LB films and giant vesicles to study GBV-C peptides interaction in the context of HIV-1 FP inhibition at membranes

Ortiz¹,

Arciniegas

Prat³

et al. 2019

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Characterization and lipid phase effect on the interaction of GBV-C E2-derived peptide, P6-2VIR576, with lipid membranes relating it with the HIV-1 FP inhibition

Cited by 3 publications

References 42 publications

Filling gaps in the knowledge of melittin on lipid membranes

Filling gaps in the knowledge of melittin on lipid membranes

Two/three-dimensional interfacial properties of the novel peptide as a selective destroyer of biomembrane

Lipid domains in LB films and giant vesicles to study GBV-C peptides interaction in the context of HIV-1 FP inhibition at membranes

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