Macromolecular analogs of the copper(II) binding site of human serum albumin. 3. Synthesis, conformation, and ion binding properties of glycylglycyl-α,γ-diaminobutyric acid derivatives of poly(L-lysine)

1986 ◽  
Vol 19 (4) ◽  
pp. 945-952 ◽  
Author(s):  
M. T. Foffani ◽  
M. Cestaro ◽  
A. Pezzoli ◽  
E. Peggion
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Ion Binding ◽  
Binding Properties ◽  
Diaminobutyric Acid ◽  
Derivatives Of

scholarly journals Effect of Common Buffers and Heterocyclic Ligands on the Binding of Cu(II) at the Multimetal Binding Site in Human Serum Albumin

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Magdalena Sokołowska ◽  
Krystyna Pawlas ◽  
Wojciech Bal
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Metal Binding ◽  
Visible Range ◽  
Heterocyclic Ligands ◽  
Binding Properties ◽  
Spectral Changes ◽  
Conformational Effects

Visible-range circular dichroism titrations were used to study Cu(II) binding properties of Multimetal Binding Site (MBS) of Human Serum Albumin (HSA). The formation of ternary MBS-Cu(II)-Buffer complexes at pH 7.4 was positively verified for sodium phosphate, Tris, and Hepes, the three most common biochemical buffers. The phosphate > Hepes > Tris order of affinities, together with strong spectral changes induced specifically by Tris, indicates the presence of both Buffer-Cu(II) and Buffer-HSA interactions. All complexes are strong enough to yield a nearly 100% ternary complex formation in 0.5 mM HSA dissolved in 100 mM solutions of respective buffers. The effects of warfarin and ibuprofen, specific ligands of hydrophobic pockets I and II in HSA on the Cu(II) binding to MBS were also investigated. The effects of ibuprofen were negligible, but warfarin diminished the MBS affinity for Cu(II) by a factor of 20, as a result of indirect conformational effects. These results indicate that metal binding properties of MBS can be modulated directly and indirectly by small molecules.

scholarly journals Chiral Derivatives of Xanthones: Investigation of the Effect of Enantioselectivity on Inhibition of Cyclooxygenases (COX-1 and COX-2) and Binding Interaction with Human Serum Albumin

2017 ◽  
Vol 10 (4) ◽  
pp. 50 ◽  
Author(s):  
Carla Fernandes ◽  
Andreia Palmeira ◽  
Inês Ramos ◽  
Carlos Carneiro ◽  
Carlos Afonso ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Interaction ◽  
Cox 2 ◽  
Derivatives Of ◽  
Cox 1
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