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Biophysical Journal 84:3138-3146 (2003)
© 2003 The Biophysical Society

A Calorimetric Study of Binary Mixtures of Dihydrosphingomyelin and Sterols, Sphingomyelin, or Phosphatidylcholine

Thomas K. M. Nyholm, Matts Nylund and J. Peter Slotte

Department of Biochemistry and Pharmacy, Åbo Akademi University, Turku, Finland

Correspondence: Address reprint requests to Thomas Nyholm, Dept. of Biochemistry and Pharmacy, Åbo Akademi University, P.O. Box 66, FIN 20521 Turku, Finland. Tel.: 3-582-215-4816; Fax: 3-582-215-4745; E-mail: thomas.nyholm{at}abo.fi.

The thermotropic properties of binary mixtures of D-erythro-n-palmitoyl-dihydrosphingomyelin (16:0-DHSM), D-erythro-n-palmitoyl-sphingomyelin (16:0-SM), cholesterol, lathosterol, and 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) were studied by differential scanning calorimetry. Addition of sterol to 16:0-DHSM and 16:0-SM bilayers resulted in a progressive decrease in both the Tm and the enthalpy of the main transition. The sterol-induced broad components in 16:0-DHSM endotherms had markedly lower enthalpies than those induced in 16:0-SM. Pretransitions recorded in 16:0-DHSM and 16:0-SM membranes responded differently to low concentrations of cholesterol. The presence of 5 mol % cholesterol increased the pretransition temperature in 16:0-SM bilayers, whereas it decreased the temperature in 16:0-DHSM membranes. Lathosterol behaved in general as cholesterol with regard to its effects on the thermotropic behavior of both sphingolipids, but it appeared to form more stable sterol-rich domains, as seen from the higher Tm of the broad component, in comparison to cholesterol. Thermograms recorded on binary mixtures of 16:0-SM:16:0-DHSM and DPPC:16:0-DHSM showed that 16:0-SM mixed nearly ideally with 16:0-DHSM, whereas DPPC mixing was less ideal in a 16:0-DHSM membrane. In conclusion, we observed that 16:0-DHSM interactions with sterols differed from that seen with 16:0-SM, and that 16:0-DHSM mixed better with 16:0-SM than DPPC, which indicates that DHSM could function as a membrane organizer within laterally condensed domains.




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