Temperature Dependence of Divalent Cation Induced Fusion of Phosphatidylserine Liposomes: Evaluation of the Kinetic Rate Constants

ORCiD

Nejat Düzgüneş: 0000-0001-6159-1391

Department

Biomedical Sciences

Document Type

Article

Publication Title

Biochemistry

ISSN

0006-2960

Volume

24

Issue

4

DOI

10.1021/bi00325a039

First Page

1064

Last Page

1072

Publication Date

2-1-1985

Abstract

The effect of temperature and divalent cation binding (Ca2+, Sr2+, Ba2+) on the kinetic rate constants of aggregation and fusion of large phosphatidylserine liposomes is measured for the first time. Fusion is monitored by the Tb3+/dipicolinate assay. Fusion rate constants increase with temperature (15-35 °C) in a roughly linear fashion. These rate constants are not otherwise sensitive to whether the temperature is above or below the phase transition temperature of the Ba2+ or Sr2+ complex of phosphatidylserine, as measured by differential scanning calorimetry. Hence, the isothermal transition of the acyl chains from liquid-crystalline to gel phase induced by the cations is not the driving force of the initial fusion event. The aggregation rate constants increase with temperature, and it is the temperature dependence of the energetics of close approach of the liposomes which underlies this increase. On the other hand, the aggregation becomes more reversible at higher temperatures, which has also been observed with monovalent cation induced liposome aggregation where there is no fusion. Calculations on several cases show that the potential energy minimum holding the liposome dimer aggregates together is ~5-6 kT deep. This result implies that the aggregation step is highly reversible; i.e., if fusion were not occurring, no stable aggregates would form. © 1985, American Chemical Society. All rights reserved.

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