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...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 35(2019), 3 vom: 22. Jan., Seite 824-830 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2019
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| 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. |
| Zusammenfassung: | 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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| Beschreibung: | Date Revised 20.11.2019 published: Print-Electronic Citation Status PubMed-not-MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.8b03718 |