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Binding interactions of niclosamide with serum proteins

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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 eVolmer and van’t Hoff equations. The binding constants and the thermodynamic parameters, DH, DS, and DG 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.

Keywords:
Fluorescence quenching Human serum albumin (HSA) Niclosamide SterneVolmer equation Thermodynamic parameters

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Ketersediaan

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Informasi Detail

Judul Seri

Journal Of Food and Drug Analysis

No. Panggil

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Penerbit

Taiwan : Elsevier Taiwan., 2014

Deskripsi Fisik

Journal Of Food and Drug Analysis 22 (2014) 549-555

Bahasa

English

ISBN/ISSN

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Klasifikasi

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Tipe Isi

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Tipe Media

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Tipe Pembawa

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Edisi

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Subjek

Food And Health

Info Detail Spesifik

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Pernyataan Tanggungjawab

Wati/Agus

Versi lain/terkait

Lampiran Berkas

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