Analysis of curcumin interaction with human serum albumin using spectroscopic studies with molecular simulation

2017 ◽  
Vol 12 (3) ◽  
pp. 199-209 ◽  
Author(s):  
Turban Kar ◽  
Pijush Basak ◽  
Srikanta Sen ◽  
Rittik Kumar Ghosh ◽  
Maitree Bhattacharyya
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Simulation ◽  
Spectroscopic Studies

Molecular Simulation and Interaction between Human Serum Albumin and Topotecan Hydrochloride

2006 ◽  
Vol 22 (12) ◽  
pp. 1456-1459
Author(s):  
LIU Yong-Ming ◽  
◽  
◽  
LI Gui-Zhi ◽  
SONG Wan-Kun ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Simulation

Equilibrium and spectroscopic studies of the ternary system: L-histidine, copper(II), and the native sequence peptide representing the copper(II)-transport site of human serum albumin

1985 ◽  
Vol 63 (11) ◽  
pp. 3117-3121 ◽  
Author(s):  
Masaaki Tabata ◽  
Bibudhendra Sarkar
Keyword(s):  
Human Serum Albumin ◽  
Ternary System ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Studies ◽  
Mixed Ligand ◽  
Anionic Form ◽  
System L ◽  
Native Sequence ◽  
Transport Site

Equilibrium and spectroscopic studies of Cu(II)-transfer of native sequence tripeptide, L-aspartyl-L-alanyl-L-histidine-N-methyl amide (AAHNMA), representing the Cu(II)-transport site of human serum albumin (HSA), and L-histidine (L-His) are reported. The equilibria in the ternary system, M–A–B (M = Cu(II), A = anionic form of AAHNMA, and B = anionic form of L-His) have been investigated by analytical potentiometry in I = 0.2 [(Na+,H+) (Cl−,OH−)] at 25 °C. The ternary system shows the presence of five mixed ligand complexes: MH2AB, MHAB, MAB, MH−1AB, and MH−2AB. The species distribution and their stability constants were evaluated by the mathematical analysis of the potentiometric data. The species were further confirmed by their individual spectra computed from the absorption measurements. At physiological pH, the equilibrium studies reveal the presence of 13% of MH−1AB (λmax = 530 nm.ε = 90 M−1 cm−1) and 3% MAB (λmax = 595 nm, ε = 97 M−1 cm−1). The combined results of equilibrium and spectroscopic studies indicate the mixed ligand complex CuH−1AB formed by deprotonation of peptide nitrogen as an important intermediate in the Cu(II)-transfer reaction. The stability constant of CuH−1AB is compared to those of other tripeptides which were designed to mimic the specific Cu(II)-transport site of human albumin.

Methyl-triclosan binding to human serum albumin: Multi-spectroscopic study and visualized molecular simulation

Chemosphere ◽  
2013 ◽  
Vol 93 (6) ◽  
pp. 1125-1130 ◽  
Author(s):  
Wenjuan Lv ◽  
Yonglei Chen ◽  
Dayong Li ◽  
Xingguo Chen ◽  
Jerzy Leszczynski
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Spectroscopic Study ◽  
Human Serum ◽  
Molecular Simulation ◽  
Methyl Triclosan
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