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

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.

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.

Molecular Interaction and Energy Transfer between Human Serum Albumin and Polyoxometalates

2007 ◽  
Vol 111 (7) ◽  
pp. 1809-1814 ◽  
Author(s):  
Guangjin Zhang ◽  
Bineta Keita ◽  
Jean-Claude Brochon ◽  
Pedro de Oliveira ◽  
Louis Nadjo ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interaction
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