Modulation of Cu2+ Binding to Sphingosine-1-Phosphate by Lipid Charge

Sphingosine-1-phosphate (S1P) is a sphingolipid metabolite that is thought to participate in the regulation of many physiological processes and may play a key role in several diseases. Herein, we found that Cu2+ binds tightly to supported lipid bilayers (SLBs) containing S1P. Specifically, we demons...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1992. - 35(2019), 3 vom: 22. Jan., Seite 824-830
1. Verfasser: Baxter, Alexis J (VerfasserIn)
Weitere Verfasser: Santiago-Ruiz, Adriana N, Yang, Tinglu, Cremer, Paul S
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2019
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, U.S. Gov't, Non-P.H.S.
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520 |a Sphingosine-1-phosphate (S1P) is a sphingolipid metabolite that is thought to participate in the regulation of many physiological processes and may play a key role in several diseases. Herein, we found that Cu2+ binds tightly to supported lipid bilayers (SLBs) containing S1P. Specifically, we demonstrated via fluorescence assays that Cu2+-S1P binding was bivalent and sensitive to the concentration of S1P in the SLB. In fact, the apparent equilibrium dissociation constant, KDApp, tightened by a factor of 132 from 4.5 μM to 34 nM as the S1P density was increased from 5.0 to 20 mol %. A major driving force for this apparent tightening was the more negative surface potential with increasing S1P concentration. This potential remained unaltered upon Cu2+ binding at pH 7.4 because two protons were released for every Cu2+ that bound. At pH 5.4, however, Cu2+ could not outcompete protons for the amine and no binding occurred. Moreover, at pH 9.4, the amine was partially deprotonated before Cu2+ binding and the surface potential became more positive on binding. The results for Cu2+-S1P binding were reminiscent of those for Cu2+-phosphatidylserine binding, where a carboxylate group helped to deprotonate the amine. In the case of S1P, however, the phosphate needed to bear two negative charges to facilitate amine deprotonation in the presence of Cu2+ 
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700 1 |a Santiago-Ruiz, Adriana N  |e verfasserin  |4 aut 
700 1 |a Yang, Tinglu  |e verfasserin  |4 aut 
700 1 |a Cremer, Paul S  |e verfasserin  |4 aut 
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