کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
30351 44471 2009 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Deciphering the perturbation of serum albumins by a ketocyanine dye: A spectroscopic approach
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
Deciphering the perturbation of serum albumins by a ketocyanine dye: A spectroscopic approach
چکیده انگلیسی

Steady state and time resolved fluorometric and circular dichroism (CD) techniques have been exploited to explore the binding interaction of a ketocyanine dye, namely, 2-[3-(N-methyl-N-phenylamino)-2-propenylidene] indanone (MPAPI) with transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA). The emission spectrum of buffered solution of the dye is found to be perturbed remarkably upon binding with the proteins. An explicit study with respect to modification of fluorescence and fluorescence anisotropy upon binding, effect of denaturant, fluorescence lifetime and CD measurements reveal that the dye binds with both BSA and HSA; the binding being stronger with the latter. Denaturation and CD studies reveal that stability of the proteins increases upon binding with the dye. The probable binding sites of the dye in the proteinous environments have been assessed from fluorescence resonance energy transfer (FRET) study. The probe is argued to be located in the inter domain cleft region of HSA (near Trp-214). From the similarity in the fluorescence behavior of the dye in BSA and HSA it is inferred that in BSA environment the probe is located near Trp-212 rather than Trp-132.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 96, Issue 2, 3 August 2009, Pages 136–143
نویسندگان
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