An intramolecular disulfide bond is essential for annexin I-mediated liposome aggregation.

Dithiothreitol (DTT) inhibits the annexin I-mediated aggregation of phosphatidylserine (PS) liposomes, but has no effect on its binding to PS vesicles. Non-reducing SDS gel analysis indicates that intermolecular disulfide bonds between annexin I molecules are not involved in liposome aggregation. However, DTT causes changes in protein conformation of annexin I as monitored by hydrophobic fluorescent dye treatment. The results suggest that the reduction of the intramolecular disulfide bond leads to inhibition of annexin I-mediated liposome aggregation via protein conformational changes.