Insight into the Binding Mechanism of Imipenem to Human Serum Albumin by Spectroscopic and Computational Approaches

2014 ◽  
Vol 11 (6) ◽  
pp. 1785-1797 ◽  
Author(s):  
Md Tabish Rehman ◽  
Hira Shamsi ◽  
Asad U. Khan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Mechanism ◽  
Computational Approaches ◽  
Insight Into

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.

Binding mechanism of tauroursodeoxycholic acid to human serum albumin: insights from NMR relaxation and docking simulations

RSC Advances ◽  
2015 ◽  
Vol 5 (15) ◽  
pp. 11036-11042 ◽  
Author(s):  
Di Wu ◽  
Yuanming Zhai ◽  
Jin Yan ◽  
Kailin Xu ◽  
Qing Wang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Nmr Relaxation ◽  
Binding Mechanism ◽  
Tauroursodeoxycholic Acid ◽  
Docking Simulations ◽  
Relationship Of

Binding patterns and structure–affinity relationship of tauroursodeoxycholic acid with human serum albumin were established by NMR methodology and docking simulations.

Chromatographic Framework to Determine the Memantine Binding Mechanism on Human Serum Albumin Surface

2008 ◽  
Vol 68 (3-4) ◽  
pp. 179-186 ◽  
Author(s):  
Firas Ibrahim ◽  
Yves-Claude Guillaume ◽  
Claire André
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Mechanism

Biophysical Insight into Furosemide Binding to Human Serum Albumin: A Study To Unveil Its Impaired Albumin Binding in Uremia

2013 ◽  
Vol 117 (9) ◽  
pp. 2595-2604 ◽  
Author(s):  
Nida Zaidi ◽  
Ejaz Ahmad ◽  
Mohd Rehan ◽  
Gulam Rabbani ◽  
Mohammad R. Ajmal ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Binding ◽  
Insight Into

Biophysical insight into the interaction of levocabastine with human serum albumin: spectroscopy and molecular docking approach

2020 ◽  
pp. 1-10
Author(s):  
Fahad M. Almutairi ◽  
Mohammad Rehan Ajmal ◽  
Mohammad Khursheed Siddiqi ◽  
Nabeela Majid ◽  
Adel Ibrahim Ahmad Al-Alawy ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Approach ◽  
Insight Into
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