scholarly journals Molecular Docking and Reaction Kinetic Studies of Chrysin Binding to Serum Albumin

2014 ◽  
Vol 9 (2) ◽  
pp. 1934578X1400900 ◽  
Author(s):  
Bingli Jiang ◽  
Anran Zhao ◽  
Jianhua Miao ◽  
Pengfei Chang ◽  
Hailin Chen ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Serum Albumin ◽  
Reaction Kinetic ◽  
Reaction Order ◽  
Kinetic Studies ◽  
Cd Spectroscopy ◽  
Reaction Enthalpy ◽  
Binding Properties ◽  
Hydrophobic Force ◽  
Physiological Conditions

The binding properties of chrysin with serum albumin (SA) were investigated under physiological conditions by calorimetry, circular dichroism (CD) spectroscopy, and molecular modeling. Based on the thermodynamic data, molar reaction enthalpy, reaction order ( n) and the rate constant ( k) were calculated. The results of CD spectroscopy showed that chrysin could bind to SA and the conformation of SA did not have any high-ordered structural change. Computational mapping revealed chrysin binding to the subdomain IB in SA. The chrysin-serum albumin complex was stabilized by hydrophobic force and hydrogen bonding and the reaction was a spontaneous process.

INFLUENCE OF QUERCETIN ON THE BINDING OF TIGECYCLINE TO HUMAN SERUM ALBUMIN

2021 ◽  
Author(s):  
Emina Mrkalić ◽  
◽  
Marina Ćendić Serafinović ◽  
Ratomir Jelić ◽  
Stefan Stojanović ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bacterial Infections ◽  
Circulatory System ◽  
Binding Properties ◽  
Free Concentration ◽  
Plant Foods ◽  
Physiological Conditions ◽  
Natural Polyphenol

Serum albumin is the major soluble protein in the circulatory system of humans. The metabolism of drugs, their distribution, free concentration, and efficacy depend on the drug-serum albumin interaction [1]. Accordingly, it is important to study the interactions of drugs with serum albumin, which determines the pharmacology and pharmacodynamics of drugs. Quercetin (QUE), a natural polyphenol widely distributed in many plant foods, such as fruits, vegetables, nuts, seeds, grains, and tea [2], bind to serum albumin [3]. Tigecycline (TGC), is a tetracycline antibiotic widely used in the treatment of bacterial infections [4]. This study aimed to investigate the binding properties of TGC to HSA in the presence of QUE, under physiological conditions, by fluorescence spectroscopy.

Investigation of the interaction of batatasin derivatives with human serum albumin using voltammetric and spectroscopic methods

RSC Advances ◽  
2016 ◽  
Vol 6 (43) ◽  
pp. 36281-36292 ◽  
Author(s):  
Jinhua Zhu ◽  
Weiping Hu ◽  
Dandan Wu ◽  
Lanlan Chen ◽  
Xiuhua Liu
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spectroscopic Methods ◽  
Binding Properties ◽  
Helix Structure ◽  
Α Helix

The binding properties of batatasin derivatives with HSA were estimated by voltammetric, spectroscopic, and molecular docking methods. There were non-electroactive complexes formed between them. And the α-helix structure in HSA was reduced.

scholarly journals The Influence of Oxidative Stress on Serum Albumin Structure as a Carrier of Selected Diazaphenothiazine with Potential Anticancer Activity

2021 ◽  
Vol 14 (3) ◽  
pp. 285
Author(s):  
Małgorzata Maciążek-Jurczyk ◽  
Beata Morak-Młodawska ◽  
Małgorzata Jeleń ◽  
Wiktoria Kopeć ◽  
Agnieszka Szkudlarek ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Anticancer Activity ◽  
Drug Distribution ◽  
Cd Spectroscopy ◽  
Drug Binding ◽  
Protein Activity ◽  
Chloramine T ◽  
The Stability

Albumin is one of the most important proteins in human blood. Among its multiple functions, drug binding is crucial in terms of drug distribution in human body. This protein undergoes many modifications that are certain to influence protein activity and affect its structure. One such reaction is albumin oxidation. Chloramine T is a strong oxidant. Solutions of human serum albumin, both non-modified and modified by chloramine T, were examined with the use of fluorescence, absorption and circular dichroism (CD) spectroscopy. 10H-3,6-diazaphenothiazine (DAPT) has anticancer activity and it has been studied for the first time in terms of binding with human serum albumin—its potential as a transporting protein. Using fluorescence spectroscopy, in the presence of dansylated amino acids, dansyl-l-glutamine (dGlu), dansyl-l-proline (dPro), DAPT binding with two main albumin sites—in subdomain IIA and IIIA—has been evaluated. Based on the conducted data, in order to measure the stability of DAPT complexes with human (HSA) and oxidized (oHSA) serum albumin, association constant (Ka) for ligand-HSA and ligand-oHSA complexes were calculated. It has been presumed that oxidation is not an important issue in terms of 10H-3,6-diazaphenothiazine binding to albumin. It means that the distribution of this substance is similar regardless of changes in albumin structure caused by oxidation, natural occurring in the organism.

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