scholarly journals The novel behaviour of interactions between Ni2+ ion and human or bovine serum albumin

1994 ◽  
Vol 304 (1) ◽  
pp. 23-26 ◽  
Author(s):  
Y Zhou ◽  
X Hu ◽  
D Ouyang ◽  
J Huang ◽  
Y Wang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Conformational Transition ◽  
Electric Dipole Transition ◽  
Molar Ratio ◽  
The Novel ◽  
Dipole Interactions ◽  
Hysteretic Effect ◽  
Hypochromic Effect

We discovered a series of novel behaviours of interactions between Ni2+ ion and human or bovine serum albumin. Our results indicated that there exist two closely neighbouring identical prior binding sites in the binding of human or bovine serum albumin with Ni2+ ions, not only one. It is very likely that, after the binding of the first Ni2+ ion, an induced slow conformational transition happens, which leads to the binding of the second Ni2+ ion and shows itself as a hysteretic effect for a process of non-enzymic protein binding with metal ions. As the concentrations of the 1:1 (molar ratio of Ni2+ ion to protein) system increase, an increasing hypochromic effect is observed. Such a hypochromic effect has not been reported previously; however, it is in accord with the mechanism of dipole-dipole interactions between the electric dipole transition moments of chromophores.

Antibodies to Indolealkylamines; Serotonin and Melatonin

1974 ◽  
Vol 52 (3) ◽  
pp. 196-202 ◽  
Author(s):  
Lee J. Grota ◽  
Gregory M. Brown
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molar Ratio ◽  
Double Immunodiffusion ◽  
Protein Conjugates ◽  
Spectrophotometric Data ◽  
Freund’S Adjuvant ◽  
Freund's Adjuvant

Serotonin, N-acetyl serotonin, and 5-methoxy-N-acetyl serotonin (melatonin) were conjugated to bovine serum albumin (BSA) using formaldehyde. The molar ratio of hapten to protein was determined spectrophotometrically. Spectrophotometric data indicated that serotonin and N-acetyl serotonin but not melatonin were conjugated to bovine serum albumin. Selected hapten–protein conjugates were suspended in Freund's adjuvant and injected into rabbits. Antisera were harvested monthly and screened by double immunodiffusion. Immunodiffusion and inhibition tests indicated that antibodies raised to serotonin–BSA reacted with serotonin and 5-methoxytryptamine but failed to cross react with N-acetyl serotonin or melatonin. Inhibition tests indicated that antibodies to N-acetyl serotonin – BSA reacted with N-acetyl serotonin and cross reacted with melatonin but not with serotonin or 5-methoxytryptamine.

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.

scholarly journals Kinetics of Vibrio cholerae sialidase action on gangliosidic substrates at different supramolecular-organizational levels

1982 ◽  
Vol 203 (3) ◽  
pp. 735-742 ◽  
Author(s):  
Bruno Venerando ◽  
Benvenuto Cestaro ◽  
Amelia Fiorilli ◽  
Riccardo Ghidoni ◽  
Augusto Preti ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Vibrio Cholerae ◽  
Bovine Serum ◽  
Mixed Micelles ◽  
Molar Ratio ◽  
Free Carbohydrates ◽  
Triton X ◽  
Kinetics Of ◽  
Vibrio Cholerae Sialidase

Gd1a, Gd1b and Gt1b gangliosides were dispersed in the following membrane-mimicking systems: (a) homogeneous micelles; (b) mixed micelles with Gm1 ganglioside (which is resistant to the enzyme action), Triton X-100 or bovine serum albumin; (c) small unilamellar vesicles of egg phosphatidylcholine. The effect of dispersion on sialic acid release by Vibrio cholerae sialidase was studied. As reference substrates freely interacting with the enzyme the lipid-free carbohydrates of Gd1a and 3′-sialosyl-lactose were employed. The apparent Vmax. of the enzyme was, with all the gangliosides, dependent on the type of ganglioside dispersion. It was lowest for homogeneous micelles and mixed micelles with ganglioside Gm1, and increased about 6-fold for ganglioside/bovine serum albumin lipoprotein micelles, 15-fold for mixed-ganglioside/Triton X-100 micelles (optimal molar ratio 1:7.5) and 30-fold for phosphatidylcholine vesicles containing 2.5 mol% ganglioside (this proportion was optimal for enzyme activity on the vesicles). For ganglioside Gd1a, the activity on Triton X-100 mixed micelles and on mixed vesicles was even greater (3- and 6-fold respectively) than that displayed on Gd1a lipid-free carbohydrate. With each of the used gangliosides the apparent Km values were very similar values for homogeneous micelles and vesicular dispersions, but showed marked increases for Triton X-100 mixed micelles, approaching the values exhibited by reference oligosaccharides. Triton X-100 micelles and phosphatidylcholine vesicles did not appreciably alter the kinetics of sialidase action on 3′-sialosyl-lactose and on Gd1a lipid-free carbohydrate, indicating that the above effects are dependent on the intrinsic characteristics of the membrane-like systems containing gangliosides.

Surface-Enhanced Raman Scattering (SERS) Spectroscopy with Borohydride-Reduced Silver Colloids: Controlling Adsorption of the Scattering Species by Surface Potential of Silver Colloid

1993 ◽  
Vol 58 (11) ◽  
pp. 2682-2694 ◽  
Author(s):  
Kateřina Čermáková ◽  
Ondřej Šesták ◽  
Pavel Matějka ◽  
Vladimír Baumruk ◽  
Blanka Vlčková
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Surface Potential ◽  
Bovine Serum ◽  
Colloidal Particles ◽  
Molar Ratio ◽  
Surface Enhanced ◽  
Surface Enhanced Raman ◽  
Enhanced Raman Scattering ◽  
Ag Colloid

Formation of Ag colloid/adsorbate SERS-active systems (upon adsorption of the selected adsorbates on the surface of Ag colloidal particles) as a function of (i) NaBH4 to AgNO3 molar ratio in the preparation protocol of Ag colloid, and (ii) aging of the colloid has been investigated by Surface-enhanced Raman scattering (SERS) spectroscopy. Oligomeric synthetic polypeptides, bovine serum albumin, phosphate coadsorbed with CuTMePyP [copper(II) derivative of 5,10,15,20-tetrakis-(N-methylpyridinium-4-yl)porphyrin chloride] and borates in systems with N-containing bases were selected as model adsorbates. Both (i) a decrease of NaBH4 to AgNO3 molar ratio upon preparation and (ii) aging of Ag colloid affect adsorption of the adsorbates and consequently, their SERS spectra, in the same manner. Aging of Ag colloid is thus viewed as a slow hydrolysis of BH4- anions. The actual concentration of BH4- in the system is identified as the most important factor controlling adsorption of all the selected adsorbates on the surface of Ag colloid. As this factor can be related to the surface potential, the conditions controlling adsorption of the selected adsorbates are specified in terms of a more negative and/or more positive surface potential of Ag colloidal particles. A more positive surface potential promotes adsorption of polypeptides, bovine serum albumin and phosphate while observation of spectral features of borates in the SERS spectra of N-containing bases in alkaline solutions is conditioned by a more negative surface potential.

Bovine Serum Albumin Interactive One Dimensional Hexanuclear Manganese (III) Complex: Synthesis, Structure, Binding and Molecular Docking Studies

2021 ◽  
Author(s):  
Mahammad Ali ◽  
Rousunara Khatun ◽  
Malay Dolai ◽  
Mihir Sasmal ◽  
Nayim Sepay
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ammonium Hydroxide ◽  
Docking Studies ◽  
Molar Ratio ◽  
One Dimensional ◽  
Molecular Docking Studies ◽  
Hexanuclear Complex

The reaction of MeO-salox (4-methoxy salicylaldehyde-oxime) with Mn(OAc)2.4H2O in methanol medium in 1:1 molar ratio and in the presence of tetra-butyl ammonium hydroxide affords a hexanuclear Complex [Mn6O2(4-MeO-salox)6(N3)2(MeOH)2(H2O)2.2H2O]n (1). Single...

scholarly journals Serum albumin enhances the uptake of [3H]cholesterol from phosphatidylcholine vesicles by cultured human fibroblasts

1984 ◽  
Vol 220 (2) ◽  
pp. 605-608 ◽  
Author(s):  
J P Slotte ◽  
S Björkerud
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Human Lung ◽  
Exchange Process ◽  
Human Fibroblasts ◽  
Lung Fibroblasts ◽  
Molar Ratio ◽  
Human Lung Fibroblasts ◽  
Cultured Human Fibroblasts

Cultured human lung fibroblasts, incubated with cholesterol/phosphatidylcholine vesicles (cholesterol: phosphatidylcholine molar ratio 1:1) incorporated vesicle [3H]-cholesterol linearly for at least 48 h by an exchange process without gaining sterol mass. The incorporation of [3H]cholesterol by the cells was markedly enhanced in the presence of purified bovine serum albumin. A fraction of the incorporated vesicle [3H]cholesterol was esterified by the cells.

scholarly journals Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin

Molecules ◽  
2018 ◽  
Vol 23 (8) ◽  
pp. 1915 ◽  
Author(s):  
Beáta Lemli ◽  
Diána Derdák ◽  
Péter Laczay ◽  
Dorottya Kovács ◽  
Sándor Kunsági-Máté
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Conformational Transition ◽  
Reaction Pathway ◽  
Noncovalent Interaction ◽  
Exchange Reactions ◽  
Serum Albumins ◽  
Adsorption Affinity ◽  
Noncovalent Binding

Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia. Adsorption affinity of tilmicosin antibiotics towards bovine serum albumin was investigated by both spectroscopic (UV-vis, Photoluminescence) and calorimetric methods. The interaction was determined on the basis of quenching of albumin by tilmicosin. Results confirm noncovalent binding of tilmicosin on bovine serum albumin with 1:1 stoichiometry associated with pK = 4.5, highlighting possible removal of tilmicosin molecules from the albumin surface through exchange reactions by known competitor molecules. Calorimetric measurements have confirmed the weak interaction between tilmicosin and albumin and reflect enhanced denaturation of the albumin in the presence of tilmicosin antibiotic. This process is associated with the decreased activation energy of conformational transition of the albumin. It opens a new, very quick reaction pathway without any significant effect on the product by noncovalent binding the tilmicosin molecules to the protein molecules. Results highlight the medical importance of these investigations by considerable docking of the selected antibiotic molecules on serum albumins. Although the binding may cause toxic effects in living bodies, the strength of the binding is weak enough to find competitor molecules for effective removals from their surface.

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