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Electrostatic interactions and complement activation on the surface of phospholipid vesicle containing acidic lipids: Effect of the structure of acidic groups: Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. In Press, Accepted Manuscript

Source: Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. In Press, Accepted Manuscript
The Acidic Domain of GPIHBP1 Is Important for the Binding of Lipoprotein Lipase and Chylomicrons: J. Biol. Chem., Vol. 283, No. 43. (24 October 2008), pp. 29554-29562.GP IHBP1, a glycosylphosph atidylinositol -anchored endothelial cell protein of the lymphocyte antigen 6 (Ly6) family, plays a key role in the lipolysis of triglyceride-r ich lipoproteins (e.g. chylomicrons). GPIHBP1 is expressed along the luminal surface of endothelial cells of heart, skeletal muscle, and adipose tissue, and GPIHBP1-expres sing cells bind lipoprotein lipase (LPL) and chylomicrons avidly. GPIHBP1 contains an amino-terminal acidic domain (amino acids 24-48) that is enriched in aspartate and glutamate residues, and we previously speculated that this domain might be important in binding ligands. To explore the functional importance of the acidic domain, we tested the ability of polyaspartate or polyglutamate peptides to block the binding of ligands to pgsA-745 Chinese hamster ovary cells that overexpress GPIHBP1. Both polyaspartate and polyglutamate blocked LPL and chylomicron binding to GPIHBP1. Also, a rabbit antiserum against the acidic domain of GPIHBP1 blocked LPL and chylomicron binding to GPIHBP1-expres sing cells. Replacing the acidic amino acids within GPIHBP1 residues 38-48 with alanine eliminated the ability of GPIHBP1 to bind LPL and chylomicrons. Finally, mutation of the positively charged heparin-bindin g domains within LPL and apolipoprotein AV abolished the ability of these proteins to bind to GPIHBP1. These studies indicate that the acidic domain of GPIHBP1 is important and that electrostatic interactions play a key role in ligand binding. 10.1074/jbc.M8 02579200

Source: J. Biol. Chem., Vol. 283, No. 43. (24 October 2008), pp. 29554-29562.
Membrane protein association by potential intramembrane charge pairs.: Nature, Vol. 351, No. 6325. (30 May 1991), pp. 414-416.The transmembrane domain of the alpha chain of the T-cell receptor is responsible both for its assembly with the CD3 delta chain and for rapid degradation of the unassembled chain within the endoplasmic reticulum. The determinant for both assembly and degradation is located in a segment of eight residues containing two basic amino acids. We show here that placement of a single basic residue in the transmembrane domain of the Tac antigen can induce interaction with the CD3 chain, through its transmembrane acidic residue. This interaction is most favoured when the interacting residues are located at the same level in the membrane. The ability to induce protein-protei n interaction by placing charge pairs within transmembrane domains suggests an approach to producing artificial dimers.

Source: Nature, Vol. 351, No. 6325. (30 May 1991), pp. 414-416.
The effect of molecular structure on hydrogen permeation and the corrosion inhibition of mild steel in acidic solutions: Corrosion Science, Vol. 37, No. 11. (November 1995), pp. 1739-1750.The influence of some triazole derivatives synthesised in the laboratory containing different hetero atoms and substituents in the organic structures on hydrogen permeation and corrosion inhibition of mild steel in acidic solutions has been studied using weight loss and various electrochemica l AC and DC corrosion monitoring techniques. All the triazole derivatives inhibit the corrosion of mild steel more effectively both in 1 N H2SO4 and 1 N HCl even at very low concentrations . Potentiodynami c polarisation studies clearly reveal that they behave predominantly as cathodic inhibitors. The extent of reduction of hydrogen permeation current through steel surface has been studied by the hydrogen electropermeat ion technique. Double layer capacitance and charge transfer resistance values were derived from Nyquist plots obtained from AC impedance studies. The adsorption of these compounds on steel surface from both the acids obeys the Temkin adsorption isotherm. UV spectral studies were also carried out to establish the actual mechanism of inhibition of corrosion.

Source: Corrosion Science, Vol. 37, No. 11. (November 1995), pp. 1739-1750.
Inhibiting and accelerating effects of aminophenols on the corrosion and permeation of hydrogen through mild steel in acidic solutions: Journal of Applied Electrochemist ry, Vol. 24, No. 4. (1 April 1994), pp. 355-360.The influence of aminophenols on the corrosion and hydrogen permeation of mild steel in 1 M HCl and 0.5 M H2SO4 has been studied using weight loss and gasometric measurements and various electrochemica l techniques. All the isomers of aminophenol inhibit the corrosion of mild steel in 1 M HC1 and accelerate it in 0.5 M H2SO4. They behave predominantly as cathodic inhibitors. Aminophenols, except PAP in I M HCI, enhance the permeation current in both the acids. The adsorption of PAP on the mild steel surface in 1 M HCl obeys the Langmuir adsorption isotherm. Surface analysis and ultraviolet spectral studies are also carried out to establish the mechanism of corrosion inhibition and acceleration of mild steel in acidic solutions.

Source: Journal of Applied Electrochemistry, Vol. 24, No. 4. (1 April 1994), pp. 355-360.
Influence of anions on the performance of isomers of aminobenzoic acid on the corrosion inhibition and hydrogen permeation through mild steel in acidic solutions: Journal of Applied Electrochemist ry, Vol. 26, No. 3. (1 March 1996), pp. 291-296.The influence of aminobenzoic acids on the corrosion and hydrogen permeation through mild steel in 1 m HC1 and 0.5 M H2SO4 has been studied using weight loss and gasometric measurements and various electrochemica l techniques. All the three isomers of aminobenzoic acid inhibit the corrosion of mild steel both in HC1 and H2SO4 in the order ortho > meta > para. It is observed that the inhibition is greater in HCI than in H2SO4. The predominant behaviour is in the cathodic inhibitor mode. These compounds reduce the permeation current in 111 HCl and enhance it in 0.51 v1 H2SO4. The adsorption of these compounds on mild steel in 1 m HC1 and 0.5 m H2SO4 obeys Langmuir's adsorption isotherm.

Source: Journal of Applied Electrochemistry, Vol. 26, No. 3. (1 March 1996), pp. 291-296.

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