Resonance Energy Transfer Between Tryptophan-214 in Human Serum Albumin and Acrylodan, Prodan, and Promen

2004 ◽  
Vol 23 (5) ◽  
pp. 351-355 ◽  
Author(s):  
José González-Jiménez ◽  
Manuel Cortijo
Keyword(s):  
Energy Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy

Resonance energy transfer between cysteine-34 and tryptophan-214 in human serum albumin. Distance measurements as a function of pH

Biochemistry ◽  
1983 ◽  
Vol 22 (10) ◽  
pp. 2415-2420 ◽  
Author(s):  
Margaret Suzukida ◽  
Hue P. Le ◽  
Fauzia Shahid ◽  
Robert A. McPherson ◽  
Edward R. Birnbaum ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Distance Measurements

Resonance energy transfer between Cys-34, Trp-214, and Tyr-411 of human serum albumin

Biochemistry ◽  
1983 ◽  
Vol 22 (10) ◽  
pp. 2420-2427 ◽  
Author(s):  
Nabil Hagag ◽  
Edward R. Birnbaum ◽  
Dennis W. Darnall
Keyword(s):  
Energy Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy

An important prerequisite for efficient Förster resonance energy transfer (FRET) from human serum albumin to alkyl gallate

RSC Advances ◽  
2016 ◽  
Vol 6 (42) ◽  
pp. 36146-36151 ◽  
Author(s):  
Qing Wang ◽  
Ying Xiao ◽  
Yanmei Huang ◽  
Hui Li
Keyword(s):  
Energy Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Specific Structure ◽  
Förster Resonance Energy Transfer ◽  
Stable Complex ◽  
Important Prerequisite

​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.

Resonance energy transfer, pH-induced folded states and the molecular interaction of human serum albumin and icariin

Luminescence ◽  
2015 ◽  
Vol 30 (7) ◽  
pp. 1026-1033 ◽  
Author(s):  
Xiao-Xia Cheng ◽  
Xiao-Yang Fan ◽  
Feng-Lei Jiang ◽  
Yi. Liu ◽  
Ke-Lin Lei
Keyword(s):  
Energy Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interaction ◽  
Resonance Energy Transfer ◽  
Resonance Energy

scholarly journals Binding of Citreoviridin to Human Serum Albumin: Multispectroscopic and Molecular Docking

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Haifeng Hou ◽  
Xiaolan Qu ◽  
Yuqin Li ◽  
Yueyue Kong ◽  
Baoxiu Jia ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Animal Health ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Apparent Distance ◽  
Wide Range ◽  
Transfer Method

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.

scholarly journals Interaction of anesthetic supplement thiopental with human serum albumin.

2008 ◽  
Vol 55 (2) ◽  
pp. 399-409 ◽  
Author(s):  
Shahper N Khan ◽  
Barira Islam ◽  
M R Rajeswari ◽  
Hammad Usmani ◽  
Asad U Khan
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Structural Changes ◽  
Resonance Energy Transfer ◽  
Drug Distribution ◽  
Resonance Energy ◽  
Albumin Concentration ◽  
Binding Interaction

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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