G. Wackerbauer et al., PREFERENTIAL PARTITIONING OF MELITTIN INTO THE AIR WATER INTERFACE - STRUCTURAL AND THERMODYNAMIC IMPLICATIONS/, Biophysical journal, 71(3), 1996, pp. 1422-1427
The membrane active agent melittin has been investigated with regard t
o the formation of a Langmuir monolayer and the accordingly induced su
rface activities, We show that in spite of its considerable solubility
in an aqueous medium, this peptide nevertheless largely accumulates i
n the air/water interface unless the lateral pressure is raised beyond
a certain threshold value depending on the pH in the subphase. The tr
ue surface concentrations have been determined by means of a recently
developed novel method based on thermodynamic principles. It affords a
n access to the partitioning equilibrium between the surface and subph
ase domains, provided the latter surrounding is not excessively prefer
red, In the present case this approach was used to derive quantitative
information on the pertinent interfacial structure and thermodynamics
, In particular, the apparent molecular area and the Gibbs energy of m
utual interaction in the monolayer could be evaluated as a function of
the applied surface pressure, The data suggest the existence of two s
tructural conversions in the course of an increasing lateral compressi
on. The surface-associated peptide accordingly assumes three different
states of successively reduced area requirements, supposedly owing to
an orientational transition involving a straightening up of a helical
conformation. This conclusion is corroborated by surface potential me
asurements reflecting corresponding changes of the effective dipole mo
ment perpendicular to the surface.