Helical Structure of Recombinant Melittin

The structure of a melittin-stabilized pore.

Melittin has been reported to form toroidal pores under certain conditions, but the atomic-resolution structure of these pores is unknown. A 9-μs all-atom molecular-dynamics simulation starting from a closely packed transmembrane melittin tetramer in DMPC shows formation of a toroidal pore after 1 μs. The pore remains stable with a roughly constant radius for the rest of the simulation. Surpris...

Quantification of the effects of melittin on liposome structure.

An optical technique, dual-polarization interferometry, has been used to examine lipid structures at the solid/liquid interface. Changes in the lipid structures, in real time, were examined as a consequence of challenging them with a peptide (melittin) that is known to induce liposome rupture. This work suggests that it should be possible to obtain a better understanding of the detail of the me...

A helical structure with Z

Antigen binding and cytotoxic properties of a recombinant immunotoxin incorporating the lytic peptide, melittin.

BACKGROUND The majority of immunotoxins studied to date incorporate toxins that act in the cytosol and thus need to be endocytosed by the target cell. An alternative strategy for immunotoxin development is the use of membrane active toxins, such as the pore-forming proteins. Melittin, a 26 amino acid cytolytic peptide from bee venom, is such a protein. OBJECTIVES We report here the constructi...

The Crystal Structure of Cholesterol Helical Ribbons

Helical ribbons form in a many multi-component solutions containing sterols similar to cholesterol, but remarkably, almost all the helices have a pitch angle of 110 or 540 . The consistent pitch angle of the ribbons may be due to an underlying crystal structure. In order to determine the crystal structure, I undertook x-ray scattering studies of individual helical ribbons taken from two particu...