Title : Thermal stability and DPPC/Ca2+ interactions of pulmonary surfactant SP-A from bulk-phase and monolayer IR spectroscopy.

Pub. Date : 2001 Nov 13

PMID : 11695915






4 Functional Relationships(s)
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1 Thermal stability and DPPC/Ca2+ interactions of pulmonary surfactant SP-A from bulk-phase and monolayer IR spectroscopy. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Homo sapiens
2 Thermal denaturation of SP-A in the presence of either DPPC or Ca2+ ion reveals a sequence of events involving the initial melting of the collagen-like region, followed by formation of intermolecular extended forms. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Homo sapiens
3 Interestingly, these spectral changes were inhibited in the ternary system, showing that the combined presence of both DPPC and Ca2+ confers a remarkable thermal stability upon SP-A. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Homo sapiens
4 The IRRAS measurements indicated that incorporation of SP-A into preformed DPPC monolayers at a surface pressure of 10 mN/m induced a decrease in the average acyl chain tilt angle from 35 degrees to 28 degrees. 1,2-Dipalmitoylphosphatidylcholine surfactant protein A1 Homo sapiens