Biophysical Journal 52: 685-692 (1987)
© 1987 the Biophysical Society

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Incorporation kinetics in a membrane, studied with the pore-forming peptide alamethicin.

Department of Biophysical Chemistry, Biocenter of the University, Basel, Switzerland.

ABSTRACT

The reaction of fluorescence-labeled alamethicin with unilamellar phospholipid vesicles (DOPC and DMPC) has been investigated in a stopped-flow apparatus. Clearly single exponential time functions have been observed at temperatures above the phase transition of the bilayer. This can be interpreted in terms of an essentially one-step incorporation process. The pseudo first-order forward rate is found to be quite fast, falling in a range somewhat below the diffusion controlled upper bound. The data are quantitatively very well described on the basis of a simple mechanism. This comprises diffusion of peptide into the bilayer accompanied by a more or less slower change of the secondary structure. Aggregation of the incorporated molecules at higher concentrations is indicated to be comparatively rapid.

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