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Biophys J, December 1999, p. 3176-3188, Vol. 77, No. 6
*Department of Physiology and Biophysics, Health Sciences Center, SUNY Stony Brook, Stony Brook, New York 11794-8661 USA; #Department of Biochemistry, Tel-Aviv University, Ramat-Aviv, Tel-Aviv 69978, Israel; and §Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032 USA
The interaction of heptalysine with vesicles formed from
mixtures of the acidic lipid phosphatidylserine (PS) and the
zwitterionic lipid phosphatidylcholine (PC) was examined experimentally
and theoretically. Three types of experiments showed that smeared charge theories (e.g., Gouy-Chapman-Stern) underestimate the membrane association when the peptide concentration is high. First, the zeta
potential of PC/PS vesicles in 100 mM KCl solution increased more
rapidly with heptalysine concentration (14.5 mV per decade) than
predicted by a smeared charge theory (6.0 mV per decade). Second,
changing the net surface charge density of vesicles by the same amount
in two distinct ways produced dramatically different effects: the molar
partition coefficient decreased 1000-fold when the mole percentage of
PS was decreased from 17% to 4%, but decreased only 10-fold when the
peptide concentration was increased to 1 µM. Third, high
concentrations of basic peptides reversed the charge on PS and PC/PS
vesicles. Calculations based on finite difference solutions to the
Poisson-Boltzmann equation applied to atomic models of heptalysine and
PC/PS membranes provide a molecular explanation for the observations: a
peptide adsorbing to the membrane in the presence of other
surface-adsorbed peptides senses a local potential more negative than
the average potential. The biological implications of these
"discreteness-of-charge" effects are discussed.
Biophys J, December 1999, p. 3176-3188, Vol. 77, No. 6
© 1999 by the Biophysical Society 0006-3495/99/12/3176/13 $2.00
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