Phosphatidylserine reversibly binds Cu2+ with extremely high affinity.
Phosphatidylserine reversibly binds Cu2+ with extremely high affinity.
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DOI:
10.1021/ja212138e
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发表时间:
2012-05-09
影响因子:
15
通讯作者:
Cremer, Paul S.
中科院分区:
文献类型:
--
作者:
Monson, Christopher F.;Cong, Xiao;Robison, Aaron D.;Pace, Hudson P.;Liu, Chunming;Poyton, Matthew F.;Cremer, Paul S.
Phosphatidylserine (PS) embedded within supported lipid bilayers (SLBs) was found to bind Cu2+ from solution with extraordinarily high affinity. In fact, the equilibrium dissociation constant was in the femtomolar range. The resulting complex formed in a 1:2 Cu2+ to PS ratio and quenches a broad spectrum of lipid-bound fluorophores in a reversible and pH-dependent fashion. At acidic pH values, the fluorophores were almost completely unquenched, while at basic pH values significant quenching (85–90%) was observed. The pH at which the transition occurred was dependent on the PS concentration and ranged from approximately pH 5 to 8. The quenching kinetics was slow at low Cu2+ concentrations and basic values pH (up to several hours), while the unquenching reaction was orders of magnitude more rapid upon lowering the pH. This was consistent with diffusion limited complex formation at basic pH, but rapid dissociation under acidic conditions. The tight binding of Cu2+ to PS may have physiological consequences under certain circumstances.
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DOI:
10.1073/pnas.1231994100
发表时间:
2003-05-27
影响因子:
11.1
作者:
Mandinov, L;Mandinova, A;Maciag, T
通讯作者:
Maciag, T
DOI:
10.1016/s0015-7368(76)71078-8
发表时间:
1976-01-01
期刊:
JOURNAL OF THE FORENSIC SCIENCE SOCIETY
影响因子:
--
作者:
CROSS, JD;LESLIE, ACD;SMITH, H
通讯作者:
SMITH, H
影响因子:
3.4
作者:
Bailey, Rachel W.;Nguyen, Thaothanh;Bell, John D.
通讯作者:
Bell, John D.
影响因子:
2.9
作者:
FEIGENSON, GW
通讯作者:
FEIGENSON, GW
影响因子:
3.4
作者:
Gal, S.;Lichtenberg, D.;Pinchuk, I.
通讯作者:
Pinchuk, I.