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

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.

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

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 Crystal Structure and Biological Implications of a Bacterial Albumin Binding Module in Complex with Human Serum Albumin

2004 ◽  
Vol 279 (41) ◽  
pp. 42924-42928 ◽  
Author(s):  
Sara Lejon ◽  
Inga-Maria Frick ◽  
Lars Björck ◽  
Mats Wikström ◽  
Stefan Svensson
Keyword(s):  
Crystal Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Albumin Binding

scholarly journals Indomethacin Increases Quercetin Affinity for Human Serum Albumin: A Combined Experimental and Computational Study and Its Broader Implications

2020 ◽  
Vol 21 (16) ◽  
pp. 5740
Author(s):  
Hrvoje Rimac ◽  
Tana Tandarić ◽  
Robert Vianello ◽  
Mirza Bojić
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Sites ◽  
Quantum Chemical ◽  
Computational Study ◽  
The Body ◽  
Active Concentration ◽  
Insight Into

Human serum albumin (HSA) is the most abundant carrier protein in the human body. Competition for the same binding site between different ligands can lead to an increased active concentration or a faster elimination of one or both ligands. Indomethacin and quercetin both bind to the binding site located in the IIA subdomain. To determine the nature of the HSA-indomethacin-quercetin interactions, spectrofluorometric, docking, molecular dynamics studies, and quantum chemical calculations were performed. The results show that the indomethacin and quercetin binding sites do not overlap. Moreover, the presence of quercetin does not influence the binding constant and position of indomethacin in the pocket. However, binding of quercetin is much more favorable in the presence of indomethacin, with its position and interactions with HSA significantly changed. These results provide a new insight into drug-drug interactions, which can be important in situations when displacement from HSA or other proteins is undesirable or even desirable. This principle could also be used to deliberately prolong or shorten the xenobiotics’ half-life in the body, depending on the desired outcomes.

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