Spectroscopic analysis of the impact of oxidative stress on the structure of human serum albumin (HSA) in terms of its binding properties

2015 ◽  
Vol 136 ◽  
pp. 265-282 ◽  
Author(s):  
M. Maciążek-Jurczyk ◽  
A. Sułkowska
Keyword(s):  
Oxidative Stress ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Analysis ◽  
Binding Properties ◽  
The Impact

scholarly journals Allysine and α-Aminoadipic Acid as Markers of the Glyco-Oxidative Damage to Human Serum Albumin under Pathological Glucose Concentrations

Antioxidants ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 474 ◽  
Author(s):  
Carolina Luna ◽  
Alexis Arjona ◽  
Carmen Dueñas ◽  
Mario Estevez
Keyword(s):  
Oxidative Stress ◽  
Plasma Concentration ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Typical Feature ◽  
Advanced Glycation ◽  
Chemical Mechanisms ◽  
Fasting Plasma ◽  
Insight Into

Understanding the molecular basis of the disease is of the utmost scientific interest as it contributes to the development of targeted strategies of prevention, diagnosis, and therapy. Protein carbonylation is a typical feature of glyco-oxidative stress and takes place in health disorders such as diabetes. Allysine as well as its oxidation product, the α-amino adipic acid (α-AA) have been found to be markers of diabetes risk whereas little is known about the chemistry involved in its formation under hyperglycemic conditions. To provide insight into this issue, human serum albumin was incubated in the presence of FeCl3 (25 μM) and increasing glucose concentrations for 32 h at 37 °C. These concentrations were selected to simulate (i) physiological fasting plasma concentration (4 mM), (ii) pathological pre-diabetes fasting plasma concentration (8 mM), and pathological diabetes fasting plasma concentration (12 mM) of glucose. While both allysine and α-AA were found to increase with increasing glucose concentrations, the carboxylic acid was only detected at pathological glucose concentrations and appeared to be a more reliable indicator of glyco-oxidative stress. The underlying chemical mechanisms of lysine glycation as well as of the depletion of tryptophan and formation of fluorescent and colored advanced glycation products are discussed.

Cigarette smoke induces alterations in the drug-binding properties of human serum albumin

2014 ◽  
Vol 52 (4) ◽  
pp. 166-174 ◽  
Author(s):  
Marco Clerici ◽  
Graziano Colombo ◽  
Francesco Secundo ◽  
Nicoletta Gagliano ◽  
Roberto Colombo ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cigarette Smoke ◽  
Drug Binding ◽  
Binding Properties

scholarly journals Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

RSC Advances ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 4742-4749 ◽  
Author(s):  
Zili Suo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
Peixiao Tang ◽  
Ruixue Gan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Simulations ◽  
Binding Properties

Probing the binding properties of trametinib to human serum albumin.

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