Simulation of the Warfarin Drug-Binding Nano-Metal Induction for Serum Albumin

2019 ◽  
Vol 10 (10) ◽  
pp. 2304
Author(s):  
Hasan Tuhmaz Hamad
Keyword(s):  
Serum Albumin ◽  
Drug Binding ◽  
Metal Induction

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.

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

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 Location of drug binding sites on human serum albumin.

1986 ◽  
Vol 34 (7) ◽  
pp. 2989-2993 ◽  
Author(s):  
KAZUO MARUYAMA ◽  
HIDEO NISHIGORI ◽  
MOTOHARU IWATSURU
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Drug Binding Sites

scholarly journals Long chain fatty acids alter the interactive binding of ligands to the two principal drug binding sites of human serum albumin

PLoS ONE ◽  
2017 ◽  
Vol 12 (6) ◽  
pp. e0180404 ◽  
Author(s):  
Keishi Yamasaki ◽  
Saya Hyodo ◽  
Kazuaki Taguchi ◽  
Koji Nishi ◽  
Noriyuki Yamaotsu ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Drug Binding ◽  
Long Chain Fatty Acids ◽  
Drug Binding Sites ◽  
Long Chain ◽  
Chain Fatty Acids

scholarly journals Probing the Sudlow binding site with warfarin: how does gold nanocluster growth alter human serum albumin?

2016 ◽  
Vol 18 (33) ◽  
pp. 22874-22878 ◽  
Author(s):  
B. A. Russell ◽  
P. A. Mulheran ◽  
D. J. S. Birch ◽  
Y. Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Gold Nanoclusters ◽  
Drug Binding ◽  
Gold Nanocluster ◽  
Drug Binding Site ◽  
Major Drug

Gold Nanoclusters (AuNCs) synthesised using Human Serum Albumin (HSA) as a stable scaffold are shown to modify the major drug binding site, Sudlow site I. Upon AuNC nucleation within HSA, warfarin was observed to no longer bind to Sudlow I, remaining free in solution.

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