Cation–Zwitterionic Lipid Interactions Are Affected by the Lateral Area per Lipid

Molecular-dynamics simulations covering 30ns of both a natural and a synthetic antimicrobial peptide in the presence of a zwitterionic lipid bilayer were performed. In both simulations, copies of the peptides were placed in an α-helical conformation on either side of the bilayer about 10Å (1Å = 0.1nm) from the interface, with either the hydrophobic or the positively charged face of the helix directed toward the bilayer surface. The degree of peptide—lipid interaction was dependent on the starting configuration: surface binding and subsequent penetration of the bilayer was observed for the hydrophobically oriented peptides, while the charge-oriented peptides demonstrated at most partial surface binding. Aromatic residues near the N-termini of the peptides appear to play an important role in driving peptide—lipid interactions. A correlation between the extent of peptide—lipid interactions and helical stability was observed in the simulations. Insertion of the peptides into the bilayer caused a dramatic increase in the lateral area per lipid and decrease in the bilayer thickness, resulting in substantial disordering of the lipid chains. Results from the simulations are consistent with early stages of proposed mechanisms for the lytic activity of antimicrobial peptides. In addition to these ‘free’ simulations, 25ns simulations were carried out with the peptides constrained at three different distances relative to the bilayer interface. The constraint forces are in agreement with the extent of peptide—bilayer insertion observed in the free simulations.

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Protein-Lipid Interactions

10.1016/s0167-7306(08)x6014-4 ◽

1993 ◽

Keyword(s):

Lipid Interactions

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Faculty Opinions recommendation of α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.717961893.793464590 ◽

2012 ◽

Author(s):

Vladimir Uversky ◽

Lizzie Atomi Pamen

Keyword(s):

Lipid Interactions

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Investigation of phospholipase-lipid interactions by optical detection of triplet state magnetic resonance spectroscopy

FEBS Letters ◽

10.1016/0014-5793(85)80743-2 ◽

1985 ◽

Vol 185 (1) ◽

pp. 71-75 ◽

Cited By ~ 4

Author(s):

Su-Yau Mao ◽

August H. Maki ◽

Gerard H. de Haas

Keyword(s):

Magnetic Resonance ◽

Magnetic Resonance Spectroscopy ◽

Triplet State ◽

Optical Detection ◽

Resonance Spectroscopy ◽

Lipid Interactions

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The relationship between protein-protein and protein-lipid interactions and the immunological properties of bovine prothrombin and several of its fragments.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)68114-7 ◽

1982 ◽

Vol 257 (4) ◽

pp. 1836-1844

Author(s):

D.A. Madar ◽

M.M. Sarasua ◽

H.C. Marsh ◽

L.G. Pedersen ◽

K.E. Gottschalk ◽

...

Keyword(s):

Immunological Properties ◽

Lipid Interactions ◽

The Relationship

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Trafficking and Association of Plasmodium falciparum MC-2TM with the Maurer’s Clefts

Pathogens ◽

10.3390/pathogens10040431 ◽

2021 ◽

Vol 10 (4) ◽

pp. 431

Author(s):

Raghavendra Yadavalli ◽

John W. Peterson ◽

Judith A. Drazba ◽

Tobili Y. Sam-Yellowe

Keyword(s):

Plasmodium Falciparum ◽

Erythrocyte Membrane ◽

Sodium Carbonate ◽

Infected Erythrocyte ◽

Brefeldin A ◽

Specific Expression ◽

Lipid Interactions ◽

And Topology ◽

Streptolysin O ◽

Maurer's Clefts

In this study, we investigated stage specific expression, trafficking, solubility and topology of endogenous PfMC-2TM in P. falciparum (3D7) infected erythrocytes. Following Brefeldin A (BFA) treatment of parasites, PfMC-2TM traffic was evaluated using immunofluorescence with antibodies reactive with PfMC-2TM. PfMC-2TM is sensitive to BFA treatment and permeabilization of infected erythrocytes with streptolysin O (SLO) and saponin, showed that the N and C-termini of PfMC-2TM are exposed to the erythrocyte cytoplasm with the central portion of the protein protected in the MC membranes. PfMC-2TM was expressed as early as 4 h post invasion (hpi), was tightly colocalized with REX-1 and trafficked to the erythrocyte membrane without a change in solubility. PfMC-2TM associated with the MC and infected erythrocyte membrane and was resistant to extraction with alkaline sodium carbonate, suggestive of protein-lipid interactions with membranes of the MC and erythrocyte. PfMC-2TM is an additional marker of the nascent MCs.

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