Experimental and theoretical investigation of water-soluble silicon(IV) phthalocyanine and its interaction with bovine serum albumin

2021 ◽  
Author(s):  
Shaya Y. Al-Raqa ◽  
Khaoula Khezami ◽  
Esra N. Kaya ◽  
Abdulkadir Kocak ◽  
Mahmut Durmuş
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Theoretical Investigation ◽  
Bovine Serum ◽  
Water Soluble ◽  
Soluble Silicon

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 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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