کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1362787 981496 2005 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
پیش نمایش صفحه اول مقاله
Interaction of cromolyn sodium with human serum albumin: A fluorescence quenching study
چکیده انگلیسی

The interaction between cromolyn sodium (CS) and human serum albumin (HSA) was investigated using tryptophan fluorescence quenching. In the discussion of the mechanism, it was proved that the fluorescence quenching of HSA by CS is a result of the formation of a CS–HSA complex. Quenching constants were determined using the Sterns–Volmer equation to provide a measure of the binding affinity between CS and HSA. The thermodynamic parameters ΔG, ΔH, and ΔS at different temperatures were calculated. The distance r between donor (Trp214) and acceptor (CS) was obtained according to fluorescence resonance energy transfer (FRET). Furthermore, synchronous fluorescence spectroscopy data and UV–vis absorbance spectra have suggested that the association between CS and HSA changed the molecular conformation of HSA and the electrostatic interactions play a major role in CS–HSA association.

An interaction between cromolyn sodium with human serum albumin was investigated by spectroscopic methods. The thermodynamic parameters at different temperatures and energy transfer parameters are provided.Figure optionsDownload as PowerPoint slide

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Bioorganic & Medicinal Chemistry - Volume 13, Issue 24, 15 December 2005, Pages 6609–6614
نویسندگان
, , , ,