scholarly journals Macromolecularization of a tripeptide analog of the Cu(II) binding site of human serum albumin. I. Synthesis, conformation, and binding properties of a Gly-Gly-His derivative of poly(L-lysine)

Biopolymers ◽  
1984 ◽  
Vol 23 (5) ◽  
pp. 985-985
Author(s):  
L. Michielin ◽  
S. Mammi ◽  
E. Peggion
2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Magdalena Sokołowska ◽  
Krystyna Pawlas ◽  
Wojciech Bal

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.


2014 ◽  
Vol 52 (4) ◽  
pp. 166-174 ◽  
Author(s):  
Marco Clerici ◽  
Graziano Colombo ◽  
Francesco Secundo ◽  
Nicoletta Gagliano ◽  
Roberto Colombo ◽  
...  

RSC Advances ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 4742-4749 ◽  
Author(s):  
Zili Suo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
Peixiao Tang ◽  
Ruixue Gan ◽  
...  

Probing the binding properties of trametinib to human serum albumin.


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