Effect of the antitumour protein alpha-sarcin on the thermotropic behaviour of acid phospholipid vesicles.
The antitumour protein alpha-sarcin modifies the thermotropic behaviour of phospholipid vesicles. This has been studied by fluorescence depolarization measurements and differential scanning calorimetry. A surface protein-phospholipid interaction is detected by measuring the polarization degree of TMA-DPH-labelled vesicles. At the higher protein/lipid molar ratios studied, the alpha-sarcin-vesicles complexes exhibit different thermotropic behaviour depending on whether they are prepared above or below the Tm of the corresponding phospholipid. Labelling of the protein with photoactive phospholipids has also been considered. alpha-Sarcin penetrates the bilayer deep enough to be labelled with the photoactive group located at the C-12 of the fatty acid acyl chain of phospholipids forming vesicles.
Gasset
M
M
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad Complutense, Madrid, Spain.
Oñaderra
M
M
Martínez del Pozo
A
A
Schiavo
G P
GP
Laynez
J
J
Usobiaga
P
P
Gavilanes
J G
JG
D000970:Antineoplastic Agents / Q000494:pharmacology*; D002152:Calorimetry, Differential Scanning; D004722:Endoribonucleases; D005454:Fluorescence Polarization; D005656:Fungal Proteins / Q000494:pharmacology*; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D013696:Temperature
D000970:Antineoplastic Agents; D005656:Fungal Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010743:Phospholipids; C014801:alpha-sarcin; D004722:Endoribonucleases