scholarly journals Investigating resonance energy transfer from protein molecules to van der Waals nanosheets

RSC Advances ◽  
2017 ◽  
Vol 7 (42) ◽  
pp. 26250-26255 ◽  
Author(s):  
Arun Singh Patel ◽  
Praveen Mishra ◽  
Pawan K. Kanaujia ◽  
Syed Shariq Husain ◽  
G. Vijaya Prakash ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Van Der Waals ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Two Dimensional ◽  
Protein Molecules ◽  
2D Nanomaterials

The resonance energy transfer (RET) from tryptophan present in bovine serum albumin (BSA) to two dimensional (2D) nanomaterials has been reported.

scholarly journals Interaction of levothyroxine with bovine serum albumin: a spectroscopic assay

2020 ◽  
Author(s):  
Nicoleta Sandu ◽  
Claudia G. Chilom ◽  
Melinda David ◽  
Monica Florescu
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Vis Spectroscopy ◽  
Ft Ir ◽  
Exogenous Compounds

ABSTRACTBovine serum albumin (BSA) acts as a carrier for many endogenous and exogenous compounds, such as thyroid hormones or corresponding drugs. Binding of the hydrophilic compound levothyroxine (LT4) to BSA can significantly alter the pharmacological properties of the compound. Therefore, studying its interaction with BSA could be a difficult issue. In this work, the binding mechanism and affinity of the interaction between LT4 and BSA were investigated, both in solution using UV-Vis, Fourier-transform infrared spectroscopy (FT-IR), fluorescence and fluorescence resonance energy transfer (FRET), as well as by Surface Plasmon Resonance (SPR) with BSA confined to a gold-coated chips, as far as we know for the first time used to study the interactions between LT4 and proteins. Quenching of BSA fluorescence by LT4 combined with UV-Vis spectroscopy shows a ground-state complex formation that may be accompanied by a nonradiative energy transfer process. FT-IR revealed the changes induced by LT4 in the secondary structure of BSA molecules, due to the partial unfolding of BSA native structure upon LT4 binding. Scatchard approach allowed the determination of the binding constant and the thermodynamic parameters, which correspond to an enthalpic process, driven mainly by hydrogen bonds and van der Waals forces. Using SPR, the adsorbed amount of biomolecules was calculated and the binding affinity of LT4 with confined-BSA was characterized using the Hill-Langmuir equation, indicating that the BSA immobilization plays an important role in LT4 binding. As preliminary results, both fluorescence quenching and SPR can be used as a stepping stone for the development of a spectroscopic biosensor for LT4 detection, with a limit of detection as low as 0.23 × 10−6 M.

scholarly journals Binding interactions and FRET between bovine serum albumin and various phenothiazine-/anthracene-based dyes: a structure–property relationship

RSC Advances ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 1679-1693
Author(s):  
Shouvik Bhuin ◽  
Sayantan Halder ◽  
Subit Kumar Saha ◽  
Manab Chakravarty
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Structure Property ◽  
Binding Interactions ◽  
Property Relationship ◽  
Structure Property Relationship

The present study demonstrates binding interactions and Förster resonance energy transfer (FRET) between bovine serum albumin (BSA) and a series of structurally and electronically diverse phenothiazine (PTZ) and anthracene (ANT) dyes.

scholarly journals Effects of metallic silver particles on resonance energy transfer in labeled bovine serum albumin

2002 ◽  
Vol 294 (4) ◽  
pp. 886-892 ◽  
Author(s):  
Joanna Malicka ◽  
Ignacy Gryczynski ◽  
Jozef Kusba ◽  
Yibing Shen ◽  
Joseph R. Lakowicz
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Metallic Silver ◽  
Silver Particles
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