A Spectroscopic Approach to Investigate the Molecular Interactions between the Newly Approved Irreversible ErbB blocker "Afatinib" and Bovine Serum Albumin

The interaction of afatinib (AFB) with bovine serum albumin (BSA) was examined via fluorescence and UV-Vis spectroscopy. Spectrofluorimetric measurements revealed that AFB can strongly quench the BSA intrinsic fluorescence through producing a non-fluorescent complex. This quenching mechanism was tho...

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Veröffentlicht in:	PloS one 2016-01, Vol.11 (1), p.e0146297-e0146297
Hauptverfasser:	Alanazi, Amer M, Abdelhameed, Ali Saber
Format:	Artikel
Sprache:	eng
Schlagworte:	Absorption spectra Afatinib Albumin Animals Binding Binding Sites Biochemistry Bovine serum albumin Cattle Chemical bonds Drugs Electrostatic bonding Electrostatic properties ErbB protein FDA approval Fluorescence Hydrophobicity Light Models, Molecular Molecular interactions Mutation Oncogene Proteins v-erbB - antagonists & inhibitors Oncogene Proteins v-erbB - chemistry Pharmaceuticals Pharmacy Physical chemistry Physiology Protein Binding Protein Conformation Protein-Tyrosine Kinases - antagonists & inhibitors Proteins Quenching Quinazolines - chemistry Serum albumin Serum Albumin, Bovine - chemistry Solution chemistry Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Spectroscopy Static Electricity Studies Temperature Thermodynamics Ultraviolet absorption
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