TY - JOUR
T1 - 201 - Binding of Cations to Phosphatidylserine Vesicles
AU - Nir, Shlomo
AU - Newton, Carolyn
AU - Papahadjopoulos, Demetrios
PY - 1978
Y1 - 1978
N2 - The binding of Ca2+ and Mg2+ to phosphatidylserine (PS) vesicles is studied experimentally and analyzed. The surface potential and charge density are found for any given concentration of both monovalent and divalent cations in solution from a modified Gouy-Chapman equation. An analytical expression is given for the amount of cations concentrated in the double-layer region, which is treated distinctly from the amount of tightly bound cations. The explanation for the binding data of Ca2+ and Mg2+ to PS required taking into account the binding of Na+ to PS. The computed binding of Na+ to PS is in accord with recent results of NMR and vesicle aggregation studies. The calculated surface potentials of PS in the presence of Ca2+ and Na+ are in a reasonable agreement with the previously measured zeta-potentials. Our results indicate that Ca2+ has a ten-fold greater intrinsic binding constant than Mg2+ for PS vesicles.
AB - The binding of Ca2+ and Mg2+ to phosphatidylserine (PS) vesicles is studied experimentally and analyzed. The surface potential and charge density are found for any given concentration of both monovalent and divalent cations in solution from a modified Gouy-Chapman equation. An analytical expression is given for the amount of cations concentrated in the double-layer region, which is treated distinctly from the amount of tightly bound cations. The explanation for the binding data of Ca2+ and Mg2+ to PS required taking into account the binding of Na+ to PS. The computed binding of Na+ to PS is in accord with recent results of NMR and vesicle aggregation studies. The calculated surface potentials of PS in the presence of Ca2+ and Na+ are in a reasonable agreement with the previously measured zeta-potentials. Our results indicate that Ca2+ has a ten-fold greater intrinsic binding constant than Mg2+ for PS vesicles.
UR - http://www.scopus.com/inward/record.url?scp=0018121962&partnerID=8YFLogxK
U2 - 10.1016/0302-4598(87)87012-5
DO - 10.1016/0302-4598(87)87012-5
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AN - SCOPUS:0018121962
SN - 0302-4598
VL - 5
SP - 116
EP - 133
JO - Bioelectrochemistry and Bioenergetics
JF - Bioelectrochemistry and Bioenergetics
IS - 1
ER -