@article {Chudzik:2016:1389-2037:198,
author = "Chudzik, Mariola and R{\’o}wnicka 128; Zubik, Joanna and Poycka, Jadwiga and Pawelczak, Bartosz and Sulkowska, Anna",
title = "Analysis of Aged Human Serum Albumin Affinity for Doxazosin",
journal = "Current Protein and Peptide Science",
volume = "17",
number = "2",
year = "2016",
publication date ="2016-03-01T00:00:00",
abstract = "Structural changes of human serum albumin (HSA) caused by old age and coexisting diseases result in differences in the binding of doxazosin (DOX). DOX is a postsynaptic 1- adrenoreceptor antagonist used for treatment of hypertension and benign prostatic hyperplasia. In elderly
people suffering from various renal or hepatic diseases the significant portion of N-form of human serum albumin (normal) is converted to A-form (aged). The differences in binding of doxazosin to N- and Aform of albumin are an important factor, which may determines therapeutic dosage and toxicity
of the test drug. To indicate these differences, the technique of fluorescence spectroscopy was used. The association constant (Ka) obtained from fluorescence quenching demonstrated that doxazosin has higher affinity for AHSA than for HSA. In order to describe the cooperativity in binding
process, the values of the Hills coefficient has been analysed. For DOX-HSA system (ex 295 nm) Hills coefficient is close to 1 and it indicates that there is a single class of binding sites. For DOX-HSA (ex 275 nm) and DOX-AHSA (ex 275 nm and ex
295 nm) systems we observed positive cooperativity (nH>1). A greater red shift of fluorescence emission maximum of AHSA than HSA in the presence of DOX was observed. This suggests that the binding of DOX to AHSA was accompanied by a stronger increase in polarity around the fluorophores
in comparison to HSA. The binding interaction between DOX and HSA has been also studied by molecular docking simulation.",
pages = "198-208",
itemtype = "ARTICLE",
parent_itemid = "infobike://ben/cpps",
issn = "1389-2037",
publishercode ="ben",
url = "http://www.ingentaconnect.com/content/ben/cpps/2016/00000017/00000002/art00014",
keyword = "molecular aging, N-A transition, human serum albumin, doxazosin"
}