scholarly journals Localization and Ordering of Lipids Around Aquaporin-0: Protein and Lipid Mobility Effects

2017 ◽  
Vol 8 ◽  
Author(s):  
Rodolfo Briones ◽  
Camilo Aponte-Santamaría ◽  
Bert L. de Groot
Keyword(s):  

2005 ◽  
Vol 127 (9) ◽  
pp. 2826-2827 ◽  
Author(s):  
Victoria Yamazaki ◽  
Oksana Sirenko ◽  
Robert J. Schafer ◽  
Jay T. Groves


Author(s):  
Abir Maarouf Kabbani ◽  
Xinxin Woodward ◽  
Christopher V. Kelly

The biophysical consequences of nanoscale curvature have been challenging to resolve due to size-dependent membrane behavior and the experimental resolution limits imposed by optical diffraction. Recent advances in nanoengineering and super-resolution techniques have enabled new capabilities for creating and observing curvature. In particular, draping supported lipid bilayers over lithographically patterned substrates provides a model system for endocytic pits. The experiments and simulations presented below describe the possible detection of membrane curvature through fluorescence recovery after photobleaching (FRAP), fluorescence correlation spectroscopy (FCS), single particle tracking (SPT), and polarized localization microscopy (PLM). FRAP and FCS depend on diffraction-limited illumination and detection. In particular, a simulation of FRAP shows no effects on lipids diffusion due to a 50 nm diameter membrane bud at any stage in the budding process. Simulated FCS demonstrated small effects due to a 50 nm radius membrane bud that was amplified with curvature-dependent lipid mobility changes. However, PLM and SPT achieve sub-diffraction-limited resolution of membrane budding and lipid mobility through the identification of the single-lipid positions with ≤15 nm spatial and ≤20 ms temporal resolution. By mapping the single-lipid step lengths to locations on the membrane, the effects of curvature on lipid behavior have been resolved.



Author(s):  
A. S. Alekseeva ◽  
P. E. Volynsky ◽  
I. A. Boldyrev

Abstract The regulation of the activity and selectivity of phospholipase A2 (PLA2), which is capable of cleaving fatty acid in the second position (sn-2) of the phospholipid, is carried out through the membrane-binding and catalytic sites of the enzyme. For hydrolytic activity, PLA2 must first bind to the phospholipid membrane, and the binding efficiency depends on the composition of the membrane. The membrane-binding site of PLA2 is formed by several tens of amino acids and its composition differs from enzyme to enzyme; hydrophobic and positively charged amino acids play a key role in the interaction. In this work, we investigated the interaction of PLA2 from bee venom with phospholipid bilayers of palmitoyl oleoylphosphatidylcholine (POPC) containing different amounts of palmitoyloleoylphosphatidylglycerol (POPG). On the basis of the measurements of the protein intrinsic fluorescence and the anisotropy of the fluorescence of the lipid probe we propose the construction of lipid–protein interaction maps, which reflect both the efficiency of protein binding and changes in the structure of the membrane. These changes cause alterations in the fluorescence anisotropy of the label, which in turn is a measure of the mobility of the lipid environment of the fluorescent probe. Analysis of interaction maps showed that there is a relationship between lipid mobility and enzyme binding efficiency: the optimum interaction of PLA2 with membranes from a POPC/POPG mixture lies in the region of the highest lipid mobility, and not in the region of the highest negative charge. This dependence complements the existing understanding of the process of recognition of the membrane surface by the enzyme and the selection of lipids by the enzyme already bound to the membrane. The proposed mapping method can be extended to other membrane-active proteins.





2002 ◽  
Vol 405 (2) ◽  
pp. 214-222 ◽  
Author(s):  
Takashi Kikukawa ◽  
Tsunehisa Araiso
Keyword(s):  




Membranes ◽  
2017 ◽  
Vol 7 (4) ◽  
pp. 60 ◽  
Author(s):  
Abir Maarouf Kabbani ◽  
Xinxin Woodward ◽  
Christopher Kelly


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