TY - JOUR
T1 - Phase and morphology changes in lipid monolayers induced by SP-B protein and its amino-terminal peptide
AU - Lipp, M. M.
AU - Lee, K. Y.C.
AU - Zasadzinski, J. A.
AU - Waring, A. J.
PY - 1996
Y1 - 1996
N2 - Both human lung surfactant protein, SP-B, and its amino-terminal peptide, SP-B1-25, inhibit the formation of condensed phases in monolayers of palmitic acid, resulting in a new fluid phase. This fluid phase forms a network, separating condensed-phase domains at coexistence. The network persists to high surface pressures, altering the nucleation, growth, and morphology of monolayer collapse structures, leading to lower surface tensions on compression and more reversible respreading on expansion. The network is stabilized by the low line tension between the fluid phase and the condensed phase as confirmed by the formation of 'stripe' phases.
AB - Both human lung surfactant protein, SP-B, and its amino-terminal peptide, SP-B1-25, inhibit the formation of condensed phases in monolayers of palmitic acid, resulting in a new fluid phase. This fluid phase forms a network, separating condensed-phase domains at coexistence. The network persists to high surface pressures, altering the nucleation, growth, and morphology of monolayer collapse structures, leading to lower surface tensions on compression and more reversible respreading on expansion. The network is stabilized by the low line tension between the fluid phase and the condensed phase as confirmed by the formation of 'stripe' phases.
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U2 - 10.1126/science.273.5279.1196
DO - 10.1126/science.273.5279.1196
M3 - Article
C2 - 8703046
AN - SCOPUS:0029789206
SN - 0036-8075
VL - 273
SP - 1196
EP - 1199
JO - Science
JF - Science
IS - 5279
ER -