Synthesis, luminescence properties of a novel aromatic carboxylic acid (L) and corresponding Eu(III) and Tb(III) compounds as well as the binding characteristics of L with bovine serum albumin (BSA)

2011 ◽  
Vol 696 (10) ◽  
pp. 2040-2046 ◽  
Author(s):  
Ruiren Tang ◽  
Chunhua Tang ◽  
Changquan Tang
Keyword(s):  
Carboxylic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Luminescence Properties ◽  
Aromatic Carboxylic Acid ◽  
Binding Characteristics

Interaction of Bis-Guanidinium Acetates Surfactants with Bovine Serum Albumin Evaluated by Spectroscopy

2021 ◽  
Vol 58 (3) ◽  
pp. 187-194
Author(s):  
Yongbo Song ◽  
Yulan Niu ◽  
Hongyan Zheng ◽  
Ying Yao
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cd Spectroscopy ◽  
Binding Characteristics ◽  
Low Concentrations ◽  
Quenching Efficiency ◽  
Hydrophobic Chain ◽  
Upward Curvature ◽  
High Concentrations

Abstract The interactions between cocopropane bis-guanidinium acetates, tallowpropane bis-guanidinium acetates with bovine serum albumin (BSA) in an aqueous solution were studied by fluorescence and circular dichroic spectroscopy measurements. The aim of the study was to elucidate the influence of the hydrophilic group and the length of the hydrophobic chain of these surfactants on the mechanism of binding to BSA. The results revealed that for both surfactants, at low concentrations, the Stern–Volmer plots had an upward curvature and at high concentrations, the quenching efficiency was decreased with increase in surfactant concentration. Different thermodynamics parameters demonstrated the existence of hydrogen bond and van der Waals force which acting as binding forces. Static quenching was observed among the protein and surfactant. The conformation of BSA was changed at higher surfactant concentrations as shown by synchronous fluorescence and CD spectroscopy. This work reveals the mechanism and binding characteristics between guanidine surfactants and protein, and provided the basis for further applications of surfactants.

Binding characteristics of bovine serum albumin encapsulated in sol-gel glasses: An alternative for protein interaction studies

2008 ◽  
Vol 373 (2) ◽  
pp. 272-280 ◽  
Author(s):  
Luz E. Vera-Avila ◽  
Erika García-Salgado ◽  
Martha P. García de Llasera ◽  
Araceli Peña-Alvarez
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interaction ◽  
Bovine Serum ◽  
Sol Gel ◽  
Binding Characteristics ◽  
Interaction Studies ◽  
Gel Glasses
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