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.

Albumin reduces basement membrane hydraulic conductance in part due to arginyl side groups

1995 ◽  
Vol 269 (5) ◽  
pp. H1514-H1521 ◽  
Author(s):  
M. A. Katz ◽  
M. L. La Marche
Keyword(s):  
Extracellular Matrix ◽  
Bovine Serum Albumin ◽  
Basement Membrane ◽  
Serum Albumin ◽  
Protective Effect ◽  
Binding Sites ◽  
Bovine Serum ◽  
Hydraulic Conductance ◽  
Experimental Control ◽  
Low Concentrations

Albumin reduces capillary hydraulic conductance (Lp) even at low concentrations. To determine if part of this barrier protective effect might be extracellular, we studied the effects of bovine serum albumin (BSA) on Lp of self-assembled basement membrane (Matrigel). Lp with tris(hydroxymethyl)aminomethane (Tris) buffer superfusate was stable at 1.77 +/- 0.22 x 10(-5) (SE) cm.s-1.cmH2O-1 over several hours. At 0.1 g/dl BSA, experimental/control (Tris) Lp fell to 83.1 +/- 6.0% (2P < 0.025), with decreases to 72.4 +/- 3.7% at 1 g/dl (2P < 0.005), 45.3 +/- 5.1% at 2.5 g/dl (2P < 0.001), and 45.0 +/- 4.8% at 4.0 g/dl (2P < 0.001). In separate experiments, BSA arginine groups were neutralized by 1,2-cyclohexanedione (CHD), and experimental/control Lp values were measured. At 2.5 g/dl, CHD-BSA depressed Lp to 54.4 +/- 4.8%, while unmodified BSA reduced Lp to 40.8 +/- 3.5% of Tris control (2P = 0.05). Finally, soluble arginine at three- and sixfold the arginine in BSA was added to BSA superfusate. For threefold, Lp rose to 120 +/- 8% of BSA level and for sixfold to 129 +/- 9% (2P < 0.05). We conclude that some part of the albumin protective effect is very likely due to consequences on extracellular matrix and that at least 18-22% of this effect is related to arginine groups on albumin when computed from Lp, and up to 34% when viscosity is taken into account. Membrane-saturable arginine-binding sites can be unbound with arginine, thus nullifying part of the barrier protective effect of BSA.

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

scholarly journals STUDIES ON ANTIBODY PRODUCTION

1963 ◽  
Vol 117 (6) ◽  
pp. 1035-1051 ◽  
Author(s):  
Maria C. Michaelides ◽  
Albert H. Coons
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Antibody Formation ◽  
Culture Fluid ◽  
Antibody Responses ◽  
Plasma Clot ◽  
Anamnestic Response ◽  
Hind Foot ◽  
High Concentrations

Rabbits were injected into the hind foot with diphtheria toxoid and bovine serum albumin. Fragments of popliteal lymph node taken from them several months later were placed in plasma-clot cultures with Eagle's medium. When antigen was added to the culture fluid, anamnestic antibody responses occurred regularly. When the antigen was diphtheria, responsiveness remained for 4 days after the beginning of the culture. When it was bovine serum albumin, responsiveness lasted for about 8 days. Once an anamnestic response had begun, antibody formation continued for 4 weeks or more. High concentrations of bovine serum albumin (0.5 mg/ml) did not inhibit the response. When both antigens were used to stimulate the same culture, it was found that the two responses were independent.

scholarly journals Hypothyroidism in rats does not lower mitochondrial ADP/O and H+/O ratios

1988 ◽  
Vol 250 (2) ◽  
pp. 477-484 ◽  
Author(s):  
R P Hafner ◽  
M D Brand
Keyword(s):  
Fatty Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Adenylate Kinase ◽  
Bovine Serum ◽  
Mitochondrial Protein ◽  
Experimental Conditions ◽  
Low Concentrations ◽  
The Difference

We investigated reports that mitochondria isolated from hypothyroid rats have decreased ADP/O and H+/O ratios. We observed no decrease in the H+/O ratio in mitochondria from hypothyroid rats, in the presence of either 2% (w/v) fatty-acid-free bovine serum albumin or 100 nM free Ca2+. The ADP/O ratio in mitochondria isolated from hypothyroid rats in the presence of 2% fatty-acid-free bovine serum albumin was measured. Under normal experimental conditions we found no decrease in the ADP/O ratio, relative to that measured for littermate controls. At the low concentrations of mitochondrial protein used in the previously reported studies, the ADP/O ratio of mitochondria from hypothyroid rats was decreased, whereas that for control rats was only slightly decreased. The difference between the ADP/O ratios measured for mitochondria form hypothyroid rats and from control rats under these conditions was eliminated by inhibition of endogenous adenylate kinase. We suggest that the lowering of the apparent ADP/O ratio in mitochondria from hypothyroid rats at low concentrations of mitochondrial protein is an experimental artefact resulting from the breakdown of ADP to AMP.

scholarly journals Conductance Changes in Bovine Serum Albumin Caused by Drug-Binding Triggered Structural Transitions

Materials ◽  
2019 ◽  
Vol 12 (7) ◽  
pp. 1022 ◽  
Author(s):  
Jing Yu ◽  
Yun Chen ◽  
Liqun Xiong ◽  
Xiaoyue Zhang ◽  
Yue Zheng
Keyword(s):  
Secondary Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cd Spectroscopy ◽  
Drug Binding ◽  
Molar Ratio ◽  
Conductive Atomic Force Microscopy ◽  
Protein Secondary Structures ◽  
Drug Concentrations

Proteins, due to their binding selectivity, are promising candidates for fabricating nanoscale bio-sensors. However, the influence of structural change on protein conductance caused by specific protein-ligand interactions and disease-induced degeneration still remains unknown. Here, we excavated the relationship between circular dichroism (CD) spectroscopy and conductive atomic force microscopy (CAFM) to reveal the effect of the protein secondary structures changes on conductance. The secondary structure of bovine serum albumin (BSA) was altered by the binding of drugs, like amoxicillin (Amox), cephalexin (Cefa), and azithromycin (Azit). The CD spectroscopy shows that the α-helical and β-sheet content of BSA, which varied according to the molar ratio between the drug and BSA, changed by up to 6%. The conductance of BSA monolayers in varying drug concentrations was further characterized via CAFM. We found that BSA conductance has a monotonic relation with α-helical content. Moreover, BSA conductance seems to be in connection with the binding ability of drugs and proteins. This work elucidates that protein conductance variations caused by secondary structure transitions are triggered by drug-binding and indicate that electrical methods are of potential application in protein secondary structure analysis.

Sign in / Sign up

Export Citation Format

Share Document