Interaction of melittin with lipid membranes

Ohki, Shinpei; Marcus, Emil; Sukumaran, Dinesh K.; Arnold, Klaus

doi:10.1016/0005-2736(94)90303-4

Cited by 75 publications

(58 citation statements)

References 41 publications

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“…However the value determined for erythrocytes may not have taken into account the continued uptake of melittin by dead cells. Alternatively, the result may be influenced by the lipid composition of the two cell types [Batenberg et al, 1988;Ohki et al, 1994].…”

Section: Discussionmentioning

confidence: 94%

Interaction of melittin with a human lymphoblastoid cell line, HMy2

Weston

Raison

1998

J. Cell. Biochem.

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We have examined the cytolytic effects of the membrane-active peptide, melittin, on a human lymphoblastoid cell line (HMy2) in the context of the use of melittin as the toxic component of an immunotoxin. The toxicity of melittin for HMy2 cells was linear over the concentration range 0.875-3.5 microM. Increased incubation times failed to result in significant cell death at concentrations of melittin below 0.875 microM. Kinetic analysis revealed that the cytolytic activity of melittin was independent of time of exposure beyond 90 min. Flow cytometric analysis of HMy2 cells incubated with FITC-labeled melittin demonstrated that the cells could incorporate up to 2.5 x 10(5) FITC-melittin molecules per cell with no reduction in viability. Extrapolation of this data indicates that 10(6) melittin molecules per cell are required for maximum cytotoxicity to HMy2 cells. Further analysis of HMy2 cells that incorporated melittin, but that remained viable, revealed that these cells were able to reduce the number of melittin molecules per cell over time. The data indicate a potential threshold value for the number of melittin molecules that may be required to be delivered to the cell surface in the form of an immunotoxin if effective selective cell death is to be achieved.

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Section: Discussionmentioning

confidence: 94%

Interaction of melittin with a human lymphoblastoid cell line, HMy2

Weston

Raison

1998

J. Cell. Biochem.

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“…Generally, the fluorescence anisotropy is characteristic of the movement rate of the fluorescent dye in the phospholipid layer, which showed no difference in the presence or absence of ERD10 and ERD14. Similarly, melittin (Ohki et al, 1994) adsorbs to the surface of the negatively charged PS membrane due to electrostatic binding and also does not change the properties of PLVs. This phenomenon, that an electrostatic adsorption does not contribute appreciably to the change of the biophysical properties of the vesicles, was also postulated before by Arnold et al (1992).…”

Section: Discussionmentioning

confidence: 99%

Chaperone Activity of ERD10 and ERD14, Two Disordered Stress-Related Plant Proteins

et al. 2008

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ERD10 and ERD14 (for early response to dehydration) proteins are members of the dehydrin family that accumulate in response to abiotic environmental stresses, such as high salinity, drought, and low temperature, in Arabidopsis (Arabidopsis thaliana). Whereas these proteins protect cells against the consequences of dehydration, the exact mode(s) of their action remains poorly understood. Here, detailed evidence is provided that ERD10 and ERD14 belong to the family of intrinsically disordered proteins, and it is shown in various assays that they act as chaperones in vitro. ERD10 and ERD14 are able to prevent the heat-induced aggregation and/or inactivation of various substrates, such as lysozyme, alcohol dehydrogenase, firefly luciferase, and citrate synthase. It is also demonstrated that ERD10 and ERD14 bind to acidic phospholipid vesicles without significantly affecting membrane fluidity. Membrane binding is strongly influenced by ionic strength. Our results show that these intrinsically disordered proteins have chaperone activity of rather wide substrate specificity and that they interact with phospholipid vesicles through electrostatic forces. We suggest that these findings provide the rationale for the mechanism of how these proteins avert the adverse effects of dehydration stresses.

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“…Although the overall antibiotic mechanisms of amphipathic antibacterial peptides having ␣-helical structure, have not been clearly elucidated, disruption of the cell structure by pore formation (14 -17) or ion channel generation seems to be the most likely mechanism (25)(26)(27). In order to investigate whether the antifungal effect of the PMAP-23 is caused by either damaging the plasma membrane or by influencing cell physiology, cells were incubated with propidium iodide (PI) (28).…”

Section: Peptide Interaction Upon the Fungal Cell Membranementioning

confidence: 99%