Fluorescence lifetime distributions of diphenylhexatrienylpropionyl-labeled phospholipids in atherogenic lipoproteins

Andreas Sommer; Roland Gorges; Gerhard M. Kostner; Fritz Paltauf; Albin Hermetter

doi:10.1117/12.58259

1 April 1992 Fluorescence lifetime distributions of diphenylhexatrienylpropionyl-labeled phospholipids in atherogenic lipoproteins

Andreas Sommer, Roland Gorges, Gerhard M. Kostner, Fritz Paltauf, Albin Hermetter

Author Affiliations +

Proceedings Volume 1640, Time-Resolved Laser Spectroscopy in Biochemistry III; (1992) https://doi.org/10.1117/12.58259
Event: OE/LASE '92, 1992, Los Angeles, CA, United States

Abstract

Fluorescent analogs of phosphatidylcholine (PC) and sphingomyelin (SM) were prepared and incorporated into the surface layer of human low-density lipoprotein (LDL) and lipoprotein (a) [Lp(a)]. Diphenylhexatrienylpropionic acid (DPH) was covalently linked to PC (DPH-PC) and SM (DPH-SM). Fluorescence lifetimes of the labeled lipoproteins were determined by phase and modulation fluorometry. Bimodal Lorentzian distributions for the decay times of DPH-PC and DPH-SM in LDL and Lp(a) were found. Lifetime distribution centers for labeled lipids were very similar except for DPH-PC in Lp(a) which was shifted to longer lifetimes. Thus, PC experiences a less polar environment in Lp(a) than in LDL. The distributional width of DPH-PC in Lp(a) was broader than in LDL. Accordingly, phosphatidylcholine must be localized in a much more homogeneous environment in LDL as compared with Lp(a). On the other hand, no difference in distributional widths was observed for DPH-SM in both lipoproteins, showing that SM organization in Lp(a) is unaffected by apo(a). From the obtained fluorescence data, it is proposed that apoprotein B preferentially associates with phosphatidylcholine.

Citation Download Citation

Andreas Sommer, Roland Gorges, Gerhard M. Kostner, Fritz Paltauf, and Albin Hermetter "Fluorescence lifetime distributions of diphenylhexatrienylpropionyl-labeled phospholipids in atherogenic lipoproteins", Proc. SPIE 1640, Time-Resolved Laser Spectroscopy in Biochemistry III, (1 April 1992); https://doi.org/10.1117/12.58259

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