scholarly journals The K-Segment of Maize DHN1 Mediates Binding to Anionic Phospholipid Vesicles and Concomitant Structural Changes

2009 ◽  
Vol 150 (3) ◽  
pp. 1503-1514 ◽  
Author(s):  
Myong-Chul Koag ◽  
Stephan Wilkens ◽  
Raymond D. Fenton ◽  
Josh Resnik ◽  
Evanly Vo ◽  
...  
Keyword(s):  
Structural Changes ◽  
Phospholipid Vesicles ◽  
Anionic Phospholipid

scholarly journals Mesoscopic Structure in the Chain-Melting Regime of Anionic Phospholipid Vesicles: DMPG

2004 ◽  
Vol 86 (6) ◽  
pp. 3722-3733 ◽  
Author(s):  
K.A. Riske ◽  
L.Q. Amaral ◽  
H.-G. Döbereiner ◽  
M.T. Lamy
Keyword(s):  
Phospholipid Vesicles ◽  
Anionic Phospholipid ◽  
Mesoscopic Structure ◽  
Melting Regime

scholarly journals The interaction of liver fatty-acid-binding protein (FABP) with anionic phospholipid vesicles: is there extended phospholipid anchorage under these conditions?

2008 ◽  
Vol 410 (1) ◽  
pp. 123-129 ◽  
Author(s):  
Robert M. Hagan ◽  
Jane Worner-Gibbs ◽  
David C. Wilton
Keyword(s):  
Fatty Acid ◽  
Fluorescence Intensity ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Phospholipid Vesicles ◽  
Anionic Phospholipid ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

Liver FABP (fatty-acid-binding protein) binds a variety of non-polar anionic ligands including fatty acids, fatty acyl CoAs, lysophospholipids and bile acids. Liver FABP is also able to bind to anionic phospholipid vesicles under conditions of low ionic strength, and membrane binding results in the release of bound ligand. However, the molecular interactions involved in binding to the phospholipid interface and the mechanism of ligand release are not known. Ligand release could be due to a significant conformational change in the protein at the interface or interaction of a phospholipid molecule with the ligand-binding cavity of the protein resulting in ligand displacement. Two portal mutant proteins of liver FABP, L28W and M74W, have now been used to investigate the binding of liver FABP to anionic phospholipid vesicles, monitoring changes in fluorescence and also fluorescence quenching in the presence of brominated lipids. There is a large increase in fluorescence intensity when the L28W mutant protein binds to vesicles prepared from DOPG (dioleoyl-sn-phosphatidylglycerol), but a large decrease in fluorescence intensity when the M74W mutant binds to these vesicles. The Br4-phospholipid prepared by bromination of DOPG dramatically quenches both L28W and M74W, consistent with the close proximity of a fatty acyl chain to the tryptophan residues. The binding of liver FABP to DOPG vesicles is accompanied by only a minimal change in the CD spectrum. Overall, the results are consistent with a molecule of anionic phospholipid interacting with the central cavity of the liver FABP, possibly involving the phospholipid molecule in an extended conformation.

Annexin A4 binding to anionic phospholipid vesicles modulated by pH and calcium

2007 ◽  
Vol 36 (4-5) ◽  
pp. 415-424 ◽  
Author(s):  
Olaf Zschörnig ◽  
Frank Opitz ◽  
Matthias Müller
Keyword(s):  
Phospholipid Vesicles ◽  
Anionic Phospholipid ◽  
Annexin A4

CTP:Phosphocholine Cytidylyltransferase Binds Anionic Phospholipid Vesicles in a Cross-Bridging Mode†

Biochemistry ◽  
2005 ◽  
Vol 44 (26) ◽  
pp. 9382-9393 ◽  
Author(s):  
Svetla G. Taneva ◽  
Philipus J. Patty ◽  
Barbara J. Frisken ◽  
Rosemary B. Cornell
Keyword(s):  
Phospholipid Vesicles ◽  
Anionic Phospholipid ◽  
Ctp:Phosphocholine Cytidylyltransferase
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