Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine studied by deuterium NMR

Dempsey, Christopher E.; Bitbol, Michel; Watts, Anthony

doi:10.1021/bi00442a009

Cited by 60 publications

(56 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, the absence of any effect of bound spectrin on the quadrupolar splittings and Ti relaxation times indicates that no significant change in the DMPS-d3 conformation or dynamics of the DMPS head group are induced by the protein, even with a large amount of spectrin (23 wt% = 0.39 x 10m3 mol%) that is similar to the physiological spectrin-lipid ratio (1O-3 mol%) [7] in the inner leaflet of the erythrocyte membrane. This result can be compared with other deuterium NMR studies of the interaction between PS and various proteins [20][21][22]301, which show that positively charged proteins which do not penetrate within the bilayer have detectable (though weak) effects on the conformation of PS head group [20,21]. Proteins which are both charged and able to penetrate into the membrane surface have a much larger effect on the conformation of PS head group [30].…”

Section: Discussionmentioning

confidence: 68%

“…The presence of charged lipids such as DMPS [28], of ions [36] or of charged anaesthetics [37] near the deuterated head group of DMPC strongly modifies its conformation, as a result of the perturbation of the bilayer surface charge [43]. Partial neutralization or screening of DMPS charges by positive charges at the membrane surface allows the DMPC head group to recover its original conformation [22]. Neutralization of the surface potential resulting from DMPS negative charges, by segmental positive charges on spectrin, thus seems to be precluded by our negative result.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A ²H and ³¹P NMR study

et al. 1989

Self Cite

View full text Add to dashboard Cite

Spectrin from human erythrocytes binds to bilayer dispersions of both DMPC and DMPSDMPC (I: 1, w/w). However, no effect of bound spectrin on the conformation of the lipid head groups, as measured from the deuterium quadrupolar splittings of DMPC or DMPS specifically deuterated in the polar head groups, was detected in I:1 mixtures of the two lipids containing either deuterated DMPC or DMPS. Neither the phase transition of the DMPS:DMPC mixtures, nor the spin-lattice relaxation time (T,) of the deuterated DMPS head group, was affected by spectrin. These results argue against any strong interaction of spectrin with phosphatidylserine and rule out the possibility that spectrin is responsible for the maintainance of PS in the inner monolayer of the erythrocyte membrane during the whole life-span of this cell.

show abstract

Section: Discussionmentioning

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A ²H and ³¹P NMR study

et al. 1989

Self Cite

View full text Add to dashboard Cite

show abstract

“…Even small variations in its geometrical orientation, however, caused by the peptide interaction would gener- ate a component in a direction normal to the membrane plane and is likely to affect significantly the magnitude of the dipole potential. In fact, studies with melittin have shown how the peptide is able to modify the orientation of the P Ϫ -N ϩ dipole (42)(43)(44). On the other hand, if part of the peptide inserts into the membrane, as described above, forming an obliquely oriented helix (26), then the direct effect of the dipolar moment of the helix must influence the membrane dipole potential.…”

Section: Figmentioning

confidence: 99%

Characterization of the Sequence of Interactions of the Fusion Domain of the Simian Immunodeficiency Virus with Membranes

Cladera

Martin

Ruysschaert

et al. 1999

Journal of Biological Chemistry

View full text Add to dashboard Cite

The simian immunodeficiency virus fusion peptide constitutes a 12-residue N-terminal segment of the gp32 protein that is involved in the fusion between the viral and cellular membranes, facilitating the penetration of the virus in the host cell. Simian immunodeficiency virus fusion peptide is a hydrophobic peptide that in Me 2 SO forms aggregates that contain ␤-sheet pleated structures. When added to aqueous media the peptide forms large colloidal aggregates. In the presence of lipidic membranes, however, the peptide interacts with the membranes and causes small changes of the membrane electrostatic potential as shown by fluorescein phosphatidylethanolamine fluorescence. Thioflavin T fluorescence and Fourier transformed infrared spectroscopy measurements reveal that the interaction of the peptide with the membrane bilayer results in complete disassembly of the aggregates originating from an Me 2 SO stock solution. Above a lipid/peptide ratio of about 5, the membrane disaggregation and water precipitation processes become dependent on the absolute peptide concentration rather than on the lipid/peptide ratio. A schematic mechanism is proposed, which sheds light on how peptide-peptide interactions can be favored with respect to peptide-lipid interactions at various lipid/peptide ratios. These studies are augmented by the use of the fluorescent dye 1-(3-sulfonatopropyl)-4-[␤[2-(di-n-octylamino)-6-naphthyl]vinyl] pyridinium betaine that shows the interaction of the peptide with the membranes has a clear effect on the magnitude of the so-called dipole potential that arises from dipolar groups located on the lipid molecules and oriented water molecules at the membrane-water interface. It is shown that the variation of the membrane dipole potential affects the extent of the membrane fusion caused by the peptide and implicates the dipolar properties of membranes in their fusion.

show abstract

“…It is well documented that the presence of negatively charged lipids in membranes, such as phosphatidylglycerol (PG), phosphatidylserine (PS), and phosphatidic acid (PA), significantly increases the melittin affinity due to attractive electrostatic interactions [38][39][40][41][42] . However, it was observed that melittin-induced bicellization of membranes was strongly hindered by the presence of anionic lipids in membranes 26,38,40,[43][44] . This observation was proposed to be due to an electrostatic anchoring of the peptide to the interface, preventing the relocation of the peptide deeper in the hydrophobic core, an essential step for the membrane fragmentation.…”

Section: Introductionmentioning

confidence: 99%

Role of the Cationic C-Terminal Segment of Melittin on Membrane Fragmentation

2016

View full text Add to dashboard Cite

The widespread distribution of cationic antimicrobial peptides capable of membrane fragmentation in nature underlines their importance to living organisms. In the present work, we determined the impact of the electrostatic interactions associated with the cationic Cterminal segment of melittin, a 26-amino acid peptide from bee venom (net charge +6), on its binding to model membranes and on the resulting fragmentation. In order to detail the role played by the C-terminal charges, we prepared a melittin analogue for which the 4 cationic amino acids in positions 21 to 24 were substituted with the polar residue citrulline, providing a peptide with the same length and amphiphilicity but with a lower net charge (+2). We compared the peptide bilayer affinity and the membrane fragmentation for bilayers prepared from dipalmitoyl-sn-glycero-3-phosphocholine (DPPC)/1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine (DPPS) mixtures. It is shown that neutralization of the C-terminal considerably increased melittin affinity for zwitterionic membranes. The unfavorable contribution associated with transferring the cationic C-terminal in a less polar environment was reduced, leaving the hydrophobic interactions, which drive the peptide insertion in bilayers, with limited counterbalancing interactions. The presence of negatively charged lipids (DPPS) in bilayers increased melittin binding by introducing attractive electrostatic interactions, the augmentation being, as expected, greater for native melittin than for its citrullinated analogue. The membrane fragmentation power of the peptide was shown to be controlled by electrostatic interactions and could be modulated by the charge carried by both the membrane and the lytic peptide. The analysis of the lipid composition of the extracted fragments from DPPC/DPPS bilayers revealed no lipid specificity. It is proposed that extended phase separations are more susceptible to lead to the extraction of a lipid species in a specific manner than a specific lipid-peptide affinity. The present work on the lipid extraction by melittin and citrullinated melittin with model membranes emphasizes the complex relation between the affinity, the lipid extraction/membrane fragmentation, and the lipid specificity.

show abstract

Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine studied by deuterium NMR

Cited by 60 publications

References 30 publications

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A ²H and ³¹P NMR study

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A ²H and ³¹P NMR study

Characterization of the Sequence of Interactions of the Fusion Domain of the Simian Immunodeficiency Virus with Membranes

Role of the Cationic C-Terminal Segment of Melittin on Membrane Fragmentation

Contact Info

Product

Resources

About

Interaction of melittin with mixed phospholipid membranes composed of dimyristoylphosphatidylcholine and dimyristoylphosphatidylserine studied by deuterium NMR

Cited by 60 publications

References 30 publications

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A 2H and 31P NMR study

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A 2H and 31P NMR study

Characterization of the Sequence of Interactions of the Fusion Domain of the Simian Immunodeficiency Virus with Membranes

Role of the Cationic C-Terminal Segment of Melittin on Membrane Fragmentation

Contact Info

Product

Resources

About

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A ²H and ³¹P NMR study

Weak interaction of spectrin with phosphatidylcholine‐phosphatidylserine multilayers: A ²H and ³¹P NMR study