The Effects of 1-Propanol on Behaviour of Human Serum Albumin in Alkaline Solution

1993 ◽  
Vol 58 (2) ◽  
pp. 267-280
Author(s):  
Vladimír Karpenko ◽  
Rostislav Škrabana
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Transition ◽  
Point Of View ◽  
Uv Spectrophotometry ◽  
Fourth Derivative ◽  
Ph Range ◽  
Albumin Molecule

The effects of 1-propanol ant to a certain extent of ethanol on human serum albumin were studied over the pH range 7 - 13.3 and alcohol concentrations up to 20 vol.%. In some case behaviour of the native preparation was compared with albumin cleared of weaker bound fatty acids. The data obtained by UV-spectrophotometry were discussed from the point of view of individual types of chromophores as well as in a broader context of the secondary structure. The results can be summarized as follows: (a) Partial removal of bound fatty acids has an influence on the dissociation of tyrosines. (b) The effect of alcohols on this dissociation is rather complex, the permitivity of the solvent being only a part of it. (c) At high alkaline pH a series of peaks in the fourth-derivative absorption spectra appear in the region 305 - 320 nm. These peaks were shown to correspond to buried dissociated tyrosines. (d) In the presence of 1-propanol a small conformational transition of albumin molecule is observed at pH below 9.

scholarly journals Characterization of the Solution Structure of Human Serum Albumin Loaded with a Metal Porphyrin and Fatty Acids

2011 ◽  
Vol 100 (9) ◽  
pp. 2293-2301 ◽  
Author(s):  
Matthias J.N. Junk ◽  
Hans W. Spiess ◽  
Dariush Hinderberger
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure ◽  
Metal Porphyrin

scholarly journals A Comprehensive Spectroscopic Analysis of the Ibuprofen Binding with Human Serum Albumin, Part II

2021 ◽  
Vol 89 (3) ◽  
pp. 30
Author(s):  
Anna Ploch-Jankowska ◽  
Danuta Pentak ◽  
Jacek E. Nycz
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Tertiary Structure ◽  
Temperature Characteristic ◽  
The Body ◽  
Structural Modifications ◽  
Influence Of Temperature On ◽  
Exogenous Substances

Human serum albumin (HSA) is the most abundant human plasma protein. HSA plays a crucial role in many binding endos- and exogenous substances, which affects their pharmacological effect. The innovative aspect of the study is not only the interaction of fatted (HSA) and defatted (dHSA) human serum albumin with ibuprofen (IBU), but the analysis of the influence of temperature on the structural modifications of albumin and the interaction between the drug and proteins from the temperature characteristic of near hypothermia (308 K) to the temperature reflecting inflammation in the body (312 K and 314 K). Ibuprofen is a non-steroidal anti-inflammatory drug. IBU is used to relieve acute pain, inflammation, and fever. To determine ibuprofen’s binding site in the tertiary structure of HSA and dHSA, fluorescence spectroscopy was used. On its basis, the fluorescent emissive spectra of albumin (5 × 10−6 mol/dm3) without and with the presence of ibuprofen (1 × 10−5–1 × 10−4 mol/dm3) was recorded. The IBU-HSA complex’s fluorescence was excited by radiation of wavelengths of λex 275 nm and λex 295 nm. Spectrophotometric spectroscopy allowed for recording the absorbance spectra (zero-order and second derivative absorption spectra) of HSA and dHSA under the influence of ibuprofen (1 × 10−4 mol/dm3). To characterize the changes of albumin structure the presence of IBU, circular dichroism was used. The data obtained show that the presence of fatty acids and human serum albumin temperature influences the strength and type of interaction between serum albumin and drug. Ibuprofen binds more strongly to defatted human serum albumin than to albumin in the presence of fatty acids. Additionally, stronger complexes are formed with increasing temperatures. The competitive binding of ibuprofen and fatty acids to albumin may influence the concentration of free drug fraction and thus its therapeutic effect.

Effects of Fatty Acids on Human Serum Albumin Binding Centers

2012 ◽  
Vol 153 (3) ◽  
pp. 323-326 ◽  
Author(s):  
G. E. Dobretsov ◽  
T. I. Syrejshchikova ◽  
N. V. Smolina ◽  
and M. G. Uzbekov
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Binding ◽  
Human Serum Albumin Binding

scholarly journals Long chain fatty acids alter the interactive binding of ligands to the two principal drug binding sites of human serum albumin

PLoS ONE ◽  
2017 ◽  
Vol 12 (6) ◽  
pp. e0180404 ◽  
Author(s):  
Keishi Yamasaki ◽  
Saya Hyodo ◽  
Kazuaki Taguchi ◽  
Koji Nishi ◽  
Noriyuki Yamaotsu ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Long Chain Fatty Acids ◽  
Drug Binding Sites ◽  
Long Chain ◽  
Chain Fatty Acids

Influence of fatty acids on the binding of calcium to human serum albumin

1977 ◽  
Vol 75 (2) ◽  
pp. 293-302 ◽  
Author(s):  
Jack H. Ladenson ◽  
Joseph C. Shyong
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum
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