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Last Updated: 3 years ago

Possible Interaction: Serum Albumin, Human and Cupric Cation

supplement:

Cupric Cation

Research Papers that Mention the Interaction

Site-selectivity studies reveal that the morin-Cu(ii) complex binds to both site 1 (subdomain IIA) and site 2 (subdomain IIIA) of human serum albumin ( HSA ) and bovine serum albumin (BSA).
Molecular bioSystems  •  2016  |  View Paper
With increasing Cu(II) concentration the Cm(III) HSA complexation is suppressed whereas the addition of Zn(II) has no effect.
Journal of inorganic biochemistry  •  2019  |  View Paper
However, in the presence of HSA , it will absorb cupric ion , which will prevent the formation of CuNPs.
Sensors  •  2017  |  View Paper
The count of the modified peptides and the … of their abundance in different samples indicated that Cu(ii ) at physiological and … concentrations inhibited HSA glycation as compared to the glycation of the Cu-devoid protein; at higher … (5 mg Cu L-1), this inhibitory effect tends to be inverted.
Metallomics : integrated biometal science  •  2017  |  View Paper
Extensive experiments showed that A-HSA altered the pathway of Cu2+ -mediated Aβ42 aggregation and protected SH-SY5Y cells from cytotoxicity and oxidative damage induced by Cu2+-Aβ42 species.
Thus, A-HSA worked as a bifunctional inhibitor against Cu2+ -mediated Aβ42 aggregation and cytotoxicity under a mildly acidic condition.
Journal of inorganic biochemistry  •  2017  |  View Paper
Furthermore, amino group and attractive electrostatic interaction of Cu(II)–ATA greatly contributed to the hydrogen bonding, van der Waals and electrostatic interaction between Cu(II)–ATA and HSA , as confirmed by experimental data.
The analysis of three-dimensional fluorescence, circular dichroism and Fourier transform infrared spectroscopy showed that Cu(II)–ATA induced the changes in the secondary structure of HSA.
JBIC Journal of Biological Inorganic Chemistry  •  2015  |  View Paper
Human serum albumin (HSA) undergoes rapid fibrillation in the presence of Cu(II) at pH 7.4 in 60% ethanol after 6-h incubation (∼65 °C) followed by room temperature incubation.
Journal of biomolecular structure & dynamics  •  2014  |  View Paper
Cuperic ion increases the stability of HSA considerably, indicating that the antioxidant property of human serum albumin are increased as a result of its interaction with cupric ion.
General physiology and biophysics  •  2014  |  View Paper
Importantly, both BSA and human serum albumin HSA ) could enhance the peroxidase-like activity of Cu2+ , which provided a new sensing platform for distinguishing BSA and HSA from other thiol-containing biomolecules.
ACS omega  •  2020  |  View Paper
The indexes of stability indicate that HSA removed Cu2+ from Aβ(1–16), rapidly, decreased Cu-induced aggregation of Aβ(1–16), and reduced the toxicity of Aβ(1–16) + Cu2+ significantly.
Bioinorganic chemistry and applications  •  2012  |  View Paper