Literature DB >> 2354169

Structure and motion of phospholipids in human plasma lipoproteins. A 31P NMR study.

D B Fenske1, R S Chana, Y I Parmar, W D Treleaven, R J Cushley.   

Abstract

The structure and motion of phospholipids in human plasma lipoproteins have been studied by using 31P NMR. Lateral diffusion coefficients, DT, obtained from the viscosity dependence of the 31P NMR line widths, were obtained for very low density lipoprotein (VLDL), low-density lipoprotein (LDL), high-density lipoproteins (HDL2, HDL3), and egg PC/TO microemulsions at 25 degrees C, for VLDL at 40 degrees C, and for LDL at 45 degrees C. At 25 degrees C, the rate of lateral diffusion in LDL (DT = 1.4 x 10(-9) cm2/s) is an order of magnitude slower than in the HDLs (DT = 2 x 10(-8) cm2/s). At 45 degrees C, DT for LDL increases to 1.1 x 10(-8) cm2/s. In contrast, DT for VLDL increases only slightly going from 25 to 40 degrees C. The large increase in diffusion rate observed in LDL occurs over the same temperature range as the smectic to disordered phase transition of the core cholesteryl esters, and provides evidence for direct interactions between the monolayer and core. In order to prove the orientation and/or order of the phospholipid head-group, estimates of the residual chemical shift anistropy, delta sigma, have been obtained for all the lipoproteins and the microemulsions from the viscosity and field dependence of the 31P NMR line widths. For VLDL and LDL, the anisotropy is 47-50 ppm at 25 degrees C, in agreement with data from phospholipid bilayers. For the HDLs, however, significantly larger values of 69-75 ppm (HDL2) and greater than 120 ppm (HDL3) were obtained.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1990        PMID: 2354169     DOI: 10.1021/bi00468a026

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  2 in total

1.  Surface properties of native human plasma lipoproteins and lipoprotein models.

Authors:  J B Massey; H J Pownall
Journal:  Biophys J       Date:  1998-02       Impact factor: 4.033

2.  Conformational changes of apoB-100 in SMase-modified LDL mediate formation of large aggregates at acidic pH.

Authors:  Mia Sneck; Su Duy Nguyen; Tero Pihlajamaa; Gebrenegus Yohannes; Marja-Liisa Riekkola; Ross Milne; Petri T Kovanen; Katariina Oörni
Journal:  J Lipid Res       Date:  2012-06-20       Impact factor: 5.922

  2 in total

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