Binding interactions of niclosamide with serum proteins
Küçük Resim Yok
Tarih
2014
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
FOOD & DRUG ADMINSTRATION
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
A study of the binding of niclosamide (NC) to serum proteins such as human serum albumin, hemoglobin, and globulin was carried out using fluorescence and UV-visible spectroscopy. Interactions between NC and these proteins were estimated by Stern-Volmer and van't Hoff equations. The binding constants and the thermodynamic parameters, Delta H, Delta S, and Delta G at different temperatures were also determined by using these equations. Data showed that NC may exhibit a static quenching mechanism with all proteins. The thermodynamic parameters were calculated. Data showed that van der Waals interactions and hydrogen bonds are the main forces for human serum albumin and hemoglobin. Globulin, however, bound to NC via hydrophobic interaction. The spectral changes of synchronous fluorescence suggested that both the microenvironment of NC and the conformation of the proteins changed in relation to their concentrations during NC's binding. Copyright (C) 2014, Food and Drug Administration, Taiwan. Published by Elsevier Taiwan LLC. All rights reserved.
Açıklama
Anahtar Kelimeler
Fluorescence quenching, Human serum albumin (HSA), Niclosamide, Stern-Volmer equation, Thermodynamic parameters
Kaynak
JOURNAL OF FOOD AND DRUG ANALYSIS
WoS Q Değeri
Q4
Scopus Q Değeri
Q1
Cilt
22
Sayı
4
