An Integrated in Silico Analysis of Drug-Binding to Human Serum Albumin

2006 ◽  
Vol 46 (6) ◽  
pp. 2709-2724 ◽  
Author(s):  
Ernesto Estrada ◽  
Eugenio Uriarte ◽  
Enrique Molina ◽  
Yamil Simón-Manso ◽  
George W. A. Milne
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico ◽  
In Silico Analysis ◽  
Drug Binding ◽  
Silico Analysis

scholarly journals An Integrated in Silico Analysis of Drug-Binding to Human Serum Albumin.

ChemInform ◽  
2007 ◽  
Vol 38 (11) ◽  
Author(s):  
Ernesto Estrada ◽  
Eugenio Uriarte ◽  
Enrique Molina ◽  
Yamil Simon-Manso ◽  
George W. A. Milne
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico ◽  
In Silico Analysis ◽  
Drug Binding ◽  
Silico Analysis

Nof2206Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: In silico and In vitro approach

2021 ◽  
pp. 116888
Author(s):  
Fahad A. Alhumaydhi ◽  
Mohammad Abdullah Aljasir ◽  
Abdullah S.M. Aljohani ◽  
Suliman A. Alsagaby ◽  
Ameen S.S. Alwashmi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico

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.

Biophysical and in silico investigations of the molecular association between a potent RNA polymerase inhibitor, thiolutin and human serum albumin

2020 ◽  
Vol 303 ◽  
pp. 112648 ◽  
Author(s):  
Md. Zahirul Kabir ◽  
Zineddine Benbekhti ◽  
Nor Farrah Wahidah Ridzwan ◽  
Rabiâa Merrouche ◽  
Noureddine Bouras ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Rna Polymerase ◽  
Human Serum ◽  
In Silico ◽  
Molecular Association ◽  
Polymerase Inhibitor
Sign in / Sign up

Export Citation Format

Share Document