We are analyzing https://link.springer.com/article/10.1007/s00775-007-0244-8.

Title:
Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity | JBIC Journal of Biological Inorganic Chemistry
Description:
The conditional stability constant at pH 7.4 for Cu(II) binding at the N-terminal site (NTS) of human serum albumin (HSA) was determined directly by competitive UV–vis spectroscopy titrations using nitrilotriacetic acid (NTA) as the competitor in 100 mM NaCl and 100 mM N-(2-hydroxyethyl)piperazine-N′-ethanesulfonic acid (Hepes). The log K NTS c value of 12.0 ± 0.1 was determined for HSA dissolved in 100 mM NaCl. A false log log K NTS c value of 11.4 ± 0.1 was obtained in the 100 mM Hepes buffer, owing to the formation of a ternary Cu(NTA)(Hepes) complex. The impact of the picomolar affinity of HSA for Cu(II) on the availability of these ions in neurodegenerative disorders is briefly discussed.
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Topics {✒️}

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Schema {🗺️}

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         description:The conditional stability constant at pH 7.4 for Cu(II) binding at the N-terminal site (NTS) of human serum albumin (HSA) was determined directly by competitive UV–vis spectroscopy titrations using nitrilotriacetic acid (NTA) as the competitor in 100 mM NaCl and 100 mM N-(2-hydroxyethyl)piperazine-N′-ethanesulfonic acid (Hepes). The log K NTS c value of 12.0 ± 0.1 was determined for HSA dissolved in 100 mM NaCl. A false log log K NTS c value of 11.4 ± 0.1 was obtained in the 100 mM Hepes buffer, owing to the formation of a ternary Cu(NTA)(Hepes) complex. The impact of the picomolar affinity of HSA for Cu(II) on the availability of these ions in neurodegenerative disorders is briefly discussed.
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      headline:Human serum albumin coordinates Cu(II) at its N-terminal binding site with 1 pM affinity
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