Binding of a Fluorescent Lipid Amphiphile to Albumin and its Transfer to Lipid Bilayer Membranes Export

@article{citeulike:4114756, abstract = {Kinetics and thermodynamics of the binding of a fluorescent lipid amphiphile, Rhodamine Green™-tetradecylamide (RG-C 14:0 ), to bovine serum albumin were characterized in an equilibrium titration and by stopped-flow fluorimetry. The binding equilibrium of RG-C 14:0 to albumin was then used to reduce its concentration in the aqueous phase to a value below its critical micelle concentration. Under these conditions, the only two species of RG-C 14:0 in the system were the monomer in aqueous solution in equilibrium with the protein-bound species. After previous determination of the kinetic and thermodynamic parameters for association of RG-C 14:0 with albumin, the kinetics of insertion of the amphiphile into and desorption off lipid bilayer membranes in different phases (solid, liquid-ordered, and liquid-disordered phases, presented as large unilamellar vesicles) were studied by stopped-flow fluorimetry at 30°C. Insertion and desorption rate constants for association of the RG-C 14:0 monomer with the lipid bilayers were used to obtain lipid/water equilibrium partition coefficients for this fluorescent amphiphile. The direct measurement of these partition coefficients is shown to provide a new method for the indirect determination of the equilibrium partition coefficient of similar molecules between two defined lipid phases if they coexist in the same membrane.}, author = {Abreu, M. and Estronca, L. and Moreno, M. and Vaz, W.}, citeulike-article-id = {4114756}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0006-3495(03)74859-0}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0006349503748590}, doi = {10.1016/S0006-3495(03)74859-0}, issn = {00063495}, journal = {Biophysical Journal}, keywords = {abreu03pdf, albumin, incorporation, lipid, membrane, transfer}, month = {January}, number = {1}, pages = {386--399}, posted-at = {2009-02-28 01:49:55}, priority = {2}, title = {Binding of a Fluorescent Lipid Amphiphile to Albumin and its Transfer to Lipid Bilayer Membranes}, url = {http://dx.doi.org/10.1016/S0006-3495(03)74859-0}, volume = {84}, year = {2003} }

TY - JOUR ID - citeulike:4114756 L3 - citeulike-article-id:4114756 N2 - Kinetics and thermodynamics of the binding of a fluorescent lipid amphiphile, Rhodamine Green™-tetradecylamide (RG-C 14:0 ), to bovine serum albumin were characterized in an equilibrium titration and by stopped-flow fluorimetry. The binding equilibrium of RG-C 14:0 to albumin was then used to reduce its concentration in the aqueous phase to a value below its critical micelle concentration. Under these conditions, the only two species of RG-C 14:0 in the system were the monomer in aqueous solution in equilibrium with the protein-bound species. After previous determination of the kinetic and thermodynamic parameters for association of RG-C 14:0 with albumin, the kinetics of insertion of the amphiphile into and desorption off lipid bilayer membranes in different phases (solid, liquid-ordered, and liquid-disordered phases, presented as large unilamellar vesicles) were studied by stopped-flow fluorimetry at 30°C. Insertion and desorption rate constants for association of the RG-C 14:0 monomer with the lipid bilayers were used to obtain lipid/water equilibrium partition coefficients for this fluorescent amphiphile. The direct measurement of these partition coefficients is shown to provide a new method for the indirect determination of the equilibrium partition coefficient of similar molecules between two defined lipid phases if they coexist in the same membrane. IS - 1 JF - Biophysical Journal SN - 00063495 EP - 399 TI - Binding of a Fluorescent Lipid Amphiphile to Albumin and its Transfer to Lipid Bilayer Membranes VL - 84 SP - 386 KW - abreu03pdf KW - albumin KW - incorporation KW - lipid KW - membrane KW - transfer AU - Abreu, M AU - Estronca, L AU - Moreno, M AU - Vaz, W PY - 2003/01// UR - http://dx.doi.org/10.1016/S0006-3495(03)74859-0 ER -