Resonance energy transfer and ligand binding studies on pH-induced folded states of human serum albumin

2008 ◽  
Vol 90 (3) ◽  
pp. 187-197 ◽  
Author(s):  
Ajay Kumar Shaw ◽  
Samir Kumar Pal
Biochemistry ◽  
1983 ◽  
Vol 22 (10) ◽  
pp. 2415-2420 ◽  
Author(s):  
Margaret Suzukida ◽  
Hue P. Le ◽  
Fauzia Shahid ◽  
Robert A. McPherson ◽  
Edward R. Birnbaum ◽  
...  

Biochemistry ◽  
1983 ◽  
Vol 22 (10) ◽  
pp. 2420-2427 ◽  
Author(s):  
Nabil Hagag ◽  
Edward R. Birnbaum ◽  
Dennis W. Darnall

RSC Advances ◽  
2016 ◽  
Vol 6 (42) ◽  
pp. 36146-36151 ◽  
Author(s):  
Qing Wang ◽  
Ying Xiao ◽  
Yanmei Huang ◽  
Hui Li

​The formation of a stable complex by fixing alkyl gallate to HSA at an appropriate orientation and distance was an important prerequisite for efficient FRET. The specific structure of HSA helped provide the selectivity of alkyl gallate.


Luminescence ◽  
2015 ◽  
Vol 30 (7) ◽  
pp. 1026-1033 ◽  
Author(s):  
Xiao-Xia Cheng ◽  
Xiao-Yang Fan ◽  
Feng-Lei Jiang ◽  
Yi. Liu ◽  
Ke-Lin Lei

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Haifeng Hou ◽  
Xiaolan Qu ◽  
Yuqin Li ◽  
Yueyue Kong ◽  
Baoxiu Jia ◽  
...  

Citreoviridin (CIT), a mycotoxin produced byPenicillium citreonigrum,is a common contaminant of wide range of agriproducts and detrimental to human and animal health. In this study, the interaction of CIT with human serum albumin (HSA) is researched by steady-state fluorescence, ultraviolet-visible (UV-Vis) absorption, circular dichroism (CD) methods, and molecular modeling. The association constants, binding site numbers, and corresponding thermodynamic parameters are used to investigate the quenching mechanism. The alternations of HSA secondary structure in the presence of CIT are demonstrated with UV-Vis, synchronous fluorescence, and CD spectra. The molecular modeling results reveal that CIT can bind with hydrophobic pocket of HSA with hydrophobic and hydrogen bond force. Moreover, an apparent distance of 3.25 nm between Trp214 and CIT is obtained via fluorescence resonance energy transfer method.


2008 ◽  
Vol 55 (2) ◽  
pp. 399-409 ◽  
Author(s):  
Shahper N Khan ◽  
Barira Islam ◽  
M R Rajeswari ◽  
Hammad Usmani ◽  
Asad U Khan

Thiopental (TPL) is a commonly used barbiturate anesthetic. Its binding with human serum albumin (HSA) was studied to explore the anesthetic-induced protein dysfunction. The basic binding interaction was studied by UV-absorption and fluorescence spectroscopy. An increase in the binding affinity (K) and in the number of binding sites (n) with the increasing albumin concentration was observed. The interaction was conformation-dependent and the highest for the F isomer of HSA, which implicates its slow elimination. The mode of binding was characterized using various thermodynamic parameters. Domain II of HSA was found to possess a high affinity binding site for TPL. The effect of micro-metal ions on the binding affinity was also investigated. The molecular distance, r, between donor (HSA) and acceptor (TPL) was estimated by fluorescence resonance energy transfer (FRET). Correlation between the stability of the TPL-N and TPL-F complexes and drug distribution is discussed. The structural changes in the protein investigated by circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy reflect perturbation of the albumin molecule and provide an explanation for the heterogeneity of action of this anesthetic.


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