Effect of ethanol or/and captopril on the secondary structure of human serum albumin before and after protein binding

2004 ◽  
Vol 57 (3) ◽  
pp. 457-464 ◽  
Author(s):  
Shan-Yang Lin ◽  
Yen-Shan Wei ◽  
Mei-Jane Li ◽  
Shun-Li Wang
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Human Serum ◽  
Before And After

The effect of Berberine on the secondary structure of human serum albumin

2005 ◽  
Vol 743 (1-3) ◽  
pp. 79-84 ◽  
Author(s):  
Ying Li ◽  
WenYing He ◽  
Jianniao Tian ◽  
Jianghong Tang ◽  
Zhide Hu ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

New Approach To Measure Protein Binding Based on a Parallel Artificial Membrane Assay and Human Serum Albumin

2008 ◽  
Vol 51 (7) ◽  
pp. 2009-2017 ◽  
Author(s):  
Elisabet Lázaro ◽  
Philip J. Lowe ◽  
Xavier Briand ◽  
Bernard Faller
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Human Serum ◽  
Artificial Membrane ◽  
New Approach

Disulfide bond cleavage of human serum albumin and alterations of its secondary structure by cis-diamminedichloroplatinum(II)

1992 ◽  
Vol 85 (1-3) ◽  
pp. 39-44 ◽  
Author(s):  
Naoko Ohta ◽  
Toshihisa Yotsuyanagi ◽  
Danni Chen ◽  
Rikako Ono ◽  
Shigekazu Ito ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bond ◽  
Bond Cleavage

Evaluation of the human serum albumin column as a discovery screening tool for plasma protein binding

2002 ◽  
Vol 15 (2) ◽  
pp. 209-215 ◽  
Author(s):  
Lisa Buchholz ◽  
Chun-Hua Cai ◽  
Larry Andress ◽  
Adriaan Cleton ◽  
Joanne Brodfuehrer ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Human Serum ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Screening Tool ◽  
Human Serum Albumin Column
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