S. Matuoka et al., CONDITION FOR THE APPEARANCE OF THE METASTABLE P-BETA' PHASE IN FULLYHYDRATED PHOSPHATIDYLCHOLINES AS STUDIES BY SMALL-ANGLE X-RAY-DIFFRACTION, Biophysical journal, 64(5), 1993, pp. 1456-1460
In the ripple phase of fully hydrated multilamellar vesicles of dipalm
itoylphosphatidylcholine (DPPC), two kinds of small-angle x-ray diffra
ction profiles are observed on cooling through the main transition. On
e is a seemingly normal profile similar to that observed on heating an
d the other is the superposition of the diffraction profiles for the p
rimary (normal) and the secondary ripple structures. We found that the
profile obtained depended on the cooling rate. Increasing the cooling
rate from 0.1-degrees-C/min to 1-degrees-C/min caused the peaks origi
nating from the secondary ripple structure to diminish. After a coolin
g scan at 43-degrees-C/min, the profile became similar to that of the
normal ripple structure, although a trace of the secondary ripple stru
cture remains. The results are interpreted in terms of the rise and fa
ll of three-dimensional correlated domains composed of both primary an
d secondary ripple structures. At slow cooling rates, correlated domai
ns of both kinds of ripple structures develop. As the cooling rate is
increased, the domain of the primary ripple structure remains correlat
ed, while that of the secondary ripple structure becomes less correlat
ed. In addition, the multipeak profile appears even at rapid cooling r
ates, if the final low temperature lies just below the T(m) for the ma
in transition. This results suggests that formation of the correlated
domains of the secondary ripple structure requires a certain time inte
rval during which the DPPC vesicles experience the temperature just be
low the main transition. The secondary ripple structure takes place in
phosphatidycholines having more than 15 carbons in each hydrocarbon c
hain upon cooling through the main transition.