Stable misfolded states of human serum albumin revealed by high-pressure infrared spectroscopic studies

2008 ◽  
Vol 37 (7) ◽  
pp. 1127-1132 ◽  
Author(s):  
L. Smeller ◽  
F. Meersman ◽  
K. Heremans
Keyword(s):  
High Pressure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Studies ◽  
Infrared Spectroscopic

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.

scholarly journals Spectroscopic Studies on the Interaction between Tilorone and Human Serum Albumin

2017 ◽  
Vol 5 (1) ◽  
pp. 48-59
Author(s):  
Alla Yegorova ◽  
Inna Leonenko ◽  
Yulia Scrypynets ◽  
Georgy Maltsev ◽  
Valery Antonovich ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Average Distance ◽  
Antiviral Drug ◽  
Fluorescence Emission ◽  
Resonance Energy ◽  
Spectroscopic Studies ◽  
Excitation Wavelength

Under physiological conditions, in vitro interaction between the antiviral drug 2,7-bis[2-(diethylamino)ethoxy]-9-fluorenone dihydrochloride (Tilorone, TIL) and human serum albumin (HSA) was investigated at excitation wavelength 280 nm and at different temperatures (298 K and 313 K) by fluorescence emission spectroscopy. TIL showed a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant is estimated as KA =7.19× 104L·mol-1 at 298 K. The enthalpy change (ΔHº) and entropy change (ΔSº) were derived to be negative values. A value of 1.63 nm for the average distance r between TIL (acceptor) and tryptophan residues of HSA (donor) was derived from the fluorescence resonance energy transfer.

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