Specific Surface Association of Avidin withN-Biotinylphosphatidylethanolamine Membrane Assemblies:  Effect on Lipid Phase Behavior and Acyl-Chain Dynamics†

Biochemistry ◽  
2001 ◽  
Vol 40 (49) ◽  
pp. 14869-14877 ◽  
Author(s):  
Musti J. Swamy ◽  
Derek Marsh
1984 ◽  
Vol 62 (11) ◽  
pp. 1134-1150 ◽  
Author(s):  
P. M. Macdonald ◽  
B. D. Sykes ◽  
R. N. McElhaney

The orientational order parameters of monofluoropalmitic acids biosynthetically incorporated into membranes of Acholeplasma laidlawii B in the presence of a large excess of a variety of structurally diverse fatty acids have been determined via 19F nuclear magnetic resonance (19F NMR) spectroscopy. It is demonstrated that these monofluoropalmitic acids are relatively nonperturbing membrane probes based upon physical (differential scanning calorimetry), biochemical (membrane lipid analysis), and biological (growth studies) criteria. 19F NMR is shown to convey the same qualitative and quantitative picture of membrane lipid order provided by 2H-NMR techniques and to be sensitive to the structural characteristics of the membrane fatty acyl chains, as well as to the lipid phase transition. Representatives of each naturally occurring class of fatty acyl chain structures, including straight-chain saturated, methyl-branched, monounsaturated, and alicyclic-ring-substituted fatty acids, were studied and the 19F-NMR order parameters were correlated with the lipid phase transitions (determined calorimetrically). The lipid phase transition was the prime determinant of overall orientational order regardless of fatty acid structure. Effects upon orientational order attributable to specific structural substituents were discernible, but were secondary to the effects of the lipid phase transition. In the gel state, relative overall order was directly proportional to the temperature of the particular lipid phase transition. Not only the overall order, but also the order profile across the membrane was sensitive to the presence of particular structural substituents. In particular, in the gel state specific fatty acyl structures demonstrated a characteristic disordering effect in the membrane order profile. These various observations can be merged to provide a unified picture of the manner in which fatty acyl chain chemistry modulates the physical state of membrane lipids.


1997 ◽  
Vol 322 (1) ◽  
pp. 49-56 ◽  
Author(s):  
Philemon PAPANASTASIOU ◽  
Malcolm J. McCONVILLE ◽  
Julie RALTON ◽  
Peter KÖHLER

The variant-specific surface proteins (VSPs) of the ancient protist Giardia duodenalis(syn.: Giardia intestinalis, Giardia lamblia) are cysteine- and threonine-rich polypeptides that can vary considerably in sequence and size. In the present study, we have purified a VSP (VSP4A1, formerly called CRISP-90) from a cloned Giardiaisolate, derived from a sheep, by Triton X-114 phase partitioning and anion-exchange chromatography. Analysis of the purified VSP4A1 showed that this protein is post-translationally modified with both glycans and lipid. The glycans of VSP4A1 were detected and partially characterized by (1) compositional analysis, which indicated the presence of GlcNAc and Glc (0.5 and 1.0 mol/mol of protein respectively), and (2) the specific labelling of VSP4A1 with galactosyltransferase/UDP-[3H]Gal. The glycans were released by β-elimination, suggesting that they are O-linked to the protein. Bio-Gel P4 chromatography of the released galactosylated glycans and further compositional analysis suggested that the major glycan on the VSP is a trisaccharide with Glc at the reducing terminus. These and other results indicate the absence of any N-linked glycans on the VSP and suggest instead that it is elaborated with a novel type of short O-linked glycan. Compositional analysis and radiolabelling experiments also indicated that VSP4A1 is modified with covalently linked palmitate (1 mol/mol of protein). Hydroxylamine treatment at neutral pH of [3H]palmitate-labelled VSP4A1 indicated that the acyl chain may be attached by a thioester linkage. A likely location for the lipid modification appears to be in the region of the C-terminal domain where it may facilitate association of the protein with the plasma membrane.


2020 ◽  
Vol 78 (2) ◽  
pp. 139-147
Author(s):  
Mariusz Duda ◽  
Kaja Cygan ◽  
Anna Wisniewska-Becker

Abstract Curcumin is a yellow–orange dye widely used as a spice, food coloring and food preservative. It also exhibits a broad range of therapeutic effects against different disorders such as cancer, diabetes, or neurodegenerative diseases. As a compound insoluble in water curcumin accumulates in cell membranes and due to this location it may indirectly lead to the observed effects by structurally altering the membrane environment. To exert strong structural effects on membrane curcumin needs to adopt a transbilayer orientation. However, there is no agreement in literature as to curcumin’s orientation and its structural effects on membranes. Here, we investigated the effects of curcumin on lipid order, lipid phase transition, and local polarity in a model liposome membranes made of DMPC or DSPC using electron paramagnetic resonance (EPR) spin labeling technique. Curcumin affected lipid order at different depths within the membrane: it slightly increased the phospholipid polar headgroup mobility as monitored by spectral parameters of T-PC, while along the acyl chain the ordering effect was observed in terms of order parameter S. Also, rotational correlation times τ2B and τ2C of 16-PC in the membrane center were increased by curcumin. Polarity measurements performed in frozen suspensions of liposomes revealed enhancement of water penetration by curcumin in the membrane center (16-PC) and in the polar headgroup region (T-PC) while the intermediate positions along the acyl chain (5-PC and 10-PC) were not significantly affected. Curcumin at a lower concentration (5 mol%) shifted the temperature of the DMPC main phase transition to lower values and increased the transition width, and at a higher concentration (10 mol%) abolished the transition completely. The observed effects suggest that curcumin adopts a transbilayer orientation within the membrane and most probably form oligomers of two molecules, each of them spanning the opposite bilayer leaflets. The effects are also discussed in terms of curcumin’s protective activity and compared with those imposed on membranes by other natural dyes known for their protective role, namely polar carotenoids, lutein and zeaxanthin.


1997 ◽  
Vol 25 (4) ◽  
pp. 261-274 ◽  
Author(s):  
R. Koynova ◽  
J. Brankov ◽  
B. Tenchov
Keyword(s):  

2005 ◽  
Vol 109 (12) ◽  
pp. 5985-5993 ◽  
Author(s):  
Julie A. Wieland ◽  
Andrew A. Gewirth ◽  
Deborah E. Leckband

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