Preparation and Application as Biosensor of Water-Soluble Conjugated Polyelectrolyte

2013 ◽  
Vol 538 ◽  
pp. 301-304
Author(s):  
Yi Ping Zhong ◽  
Rui Bin Hong ◽  
Bin Bin Yin ◽  
Ping Liu ◽  
Wen Ji Deng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Conjugated Polyelectrolyte ◽  
Sodium Sulfonate ◽  
Vis Spectroscopy

The water-soluble conjugated polyelectrolyte, poly[3-(1′-propyloxy-3′-sodium sulfonate) thiophene] (PTH-n3-SO3Na), was prepared. The interaction between the PTH-n3-SO3Na and bovine serum albumin (BSA) was investigated using UV-vis spectroscopy. It was found that the PTH-n3-SO3Na could be used as biosensor to detect BSA.

scholarly journals Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Materials ◽  
2021 ◽  
Vol 14 (2) ◽  
pp. 298
Author(s):  
Shufang Liu ◽  
Shu’e Wang ◽  
Zhanzuo Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Inner Filter Effect ◽  
Spectroscopic Techniques ◽  
Size Distributions ◽  
Size Dependent ◽  
Filter Effect ◽  
Vis Spectroscopy

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

scholarly journals Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

2013 ◽  
Vol 36 (1-2) ◽  
pp. 21-26 ◽  
Author(s):  
Hamid Dezhampanah ◽  
Abdol-Khalegh Bordbar ◽  
Yadolahe Khodadusdt
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Conformation ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Aggregate Formation ◽  
Cationic Porphyrin ◽  
Porphyrin Complex ◽  
Induced Aggregation

The interaction of a water-soluble cationic porphyrin, Cobalt(III) 5, 10, 15, 20-tetrakis (1-methylpyridinium-4-yl) porphyrin [Co(III)TMPyP], with bovine serum albumin (BSA) has been studied in 1 mM phosphate buffer pH 7.0 containing 5 mM NaCl by UV-vis absorption, resonance light scattering (RLS) and fluorescence spectroscopies at 25°C. The results of RLS studies represent no aggregate formation of porphyrin in the surface of BSA and low tendency of this porphyrin for aggregate formation.The binding of porphyrin complex to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The values of Stern-Volmer constants, KSV, was determined nearly 105M−1, that depend on BSA concentration. The average aggregation number of BSA calculated from the analysis of fluorescence quenching data indicates that absence of any porphyrin induced aggregation of BSA due to its interaction with porphyrin complex. The binding of Co(III) TMPyP had no obvious effect on the molecular conformation of the protein. Electrostatic force played an important role in the binding due to the opposite charges on porphyrin and the protein.

Synthesis of Water-Soluble Red-Emitting Thienyl-BODIPYs and Bovine Serum Albumin Labeling

2014 ◽  
Vol 20 (5) ◽  
pp. 1252-1257 ◽  
Author(s):  
Arnaud Poirel ◽  
Pascal Retailleau ◽  
Antoinette De Nicola ◽  
Raymond Ziessel
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble
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