کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1231817 1495263 2013 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Binding of naproxen enantiomers to human serum albumin studied by fluorescence and room-temperature phosphorescence
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
Binding of naproxen enantiomers to human serum albumin studied by fluorescence and room-temperature phosphorescence
چکیده انگلیسی

The interaction of the enantiomers of the non-steroidal anti-inflammatory drug naproxen (NPX) with human serum albumin (HSA) has been investigated using fluorescence and phosphorescence spectroscopy in the steady-state and time-resolved mode. The absorption, fluorescence excitation, and fluorescence emission spectra of (S)-NPX and (R)-NPX differ in shape in the presence of HSA, indicating that these enantiomers experience a different environment when bound. In solutions containing 0.2 M KI, complexation with HSA results in a strongly increased NPX fluorescence intensity and a decreased NPX phosphorescence intensity due to the inhibition of the collisional interaction with the heavy atom iodide. Fluorescence intensity curves obtained upon selective excitation of NPX show 8-fold different slopes for bound and free NPX. No significant difference in the binding constants of (3.8 ± 0.6) × 105 M−1 for (S)-NPX and (3.9 ± 0.6) × 105 M−1 for (R)-NPX was found. Furthermore, the addition of NPX quenches the phosphorescence of the single tryptophan in HSA (Trp-214) based on Dexter energy transfer. The short-range nature of this mechanism explains the upward curvature of the Stern–Volmer plot observed for HSA: At low concentrations NPX binds to HSA at a distance from Trp-214 and no quenching occurs, whereas at high NPX concentrations the phosphorescence intensity decreases due to dynamic quenching by NPX diffusing into site I from the bulk solution. The dynamic quenching observed in the Stern–Volmer plots based on the longest phosphorescence lifetime indicates an overall binding constant to HSA of about 3 × 105 M−1 for both enantiomers.

Static and dynamic interactions of HSA with the drugs (S)- or (R)-naproxen studied with phosphorescence and fluorescence.Figure optionsDownload as PowerPoint slideHighlights
► Fluorescence spectra of (S)- and (R)-naproxen show enantioselective binding to HSA.
► Dynamics were studied at ns (fluorescence) to ms (phosphorescence) timescales.
► (S)- and (R)-naproxen bound to HSA are effectively shielded from iodide quenching.
► Phosphorescence of HSA showed 1:1 binding, followed by dynamic quenching.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy - Volume 105, 15 March 2013, Pages 67–73
نویسندگان
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