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.

scholarly journals Effect of Bovine Serum Albumin on Redox and Ligand Exchange Reactions Involving Aquacobalamin

2020 ◽  
Vol 13 (3) ◽  
pp. 223-228
Author(s):  
Ilia A. Dereven’kov ◽  
Sergei V. Makarov ◽  
Pavel A. Molodtsov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ligand Exchange ◽  
Bovine Serum ◽  
Exchange Reactions

scholarly journals Fluorescence Spectroscopy Study on the Interaction between Evodiamine and Bovine Serum Albumin

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Mingxiong Tan ◽  
Weijiang Liang ◽  
Xujian Luo ◽  
Yunqiong Gu
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Association Constants ◽  
Experimental Results ◽  
Spectroscopy Study ◽  
Serum Albumins ◽  
Two Temperatures

The interaction of evodiamine (Evo) with bovine serum albumins (BSAs) at different two temperatures (298 and 310 K) was investigated by means of fluorescence spectroscopy. The experimental results showed that Evo binds with BSA via a static quenching procedure with association constantsKof1.61×106 L/mol at 298 K and6.78×105 L/mol at 310 K. The number of bound Evo molecules per protein is 1.31 at 298 K and 1.33 at 310 K. The results suggested that Evo reacts with BSA chiefly through hydrophobic and electrostatic interactions, and it does not alter theα-helical nature of BAS.

scholarly journals Interaction of dinitrophenyl groups bound to bovine serum albumin with univalent fragments of anti-dinitrophenyl antibody

1979 ◽  
Vol 177 (1) ◽  
pp. 225-236 ◽  
Author(s):  
C. Graham Knight ◽  
N. Michael Green
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Deae Cellulose ◽  
Serum Albumins ◽  
Single Polypeptide Chain ◽  
Quenching Efficiency ◽  
Lysine Residues ◽  
Single Polypeptide

Two lysine residues of bovine serum albumin reacted with 1-fluoro-2,4-dinitrobenzene with apparent second-order rate constants approx. 500-times greater than those observed in similar reactions with low-molecular-weight lysine derivatives. A series of dinitrophenyl (Dnp)-bovine serum albumins were prepared and their ability to bind univalent fragments of anti-Dnp antibody was measured by fluorescence-quenching titrations. Compared with the Dnp group of the free hapten, 6-N-Dnp-aminohexanoate, the majority of the protein-bound Dnp groups were unavailable to the antibody at pH8.0. When the same Dnp-albumins were titrated at pH3.0 the availability of the Dnp groups increased approx. 3-fold. Dnp-albumins were treated with pepsin at pH3.0 and Dnp-containing fragments isolated by chromatography on DE-52 DEAE-cellulose. Fluorescence-quenching titrations showed that the Dnp groups on the fragments behaved like the free hapten with respect to quenching efficiency, although with an increased dissociation constant. The association between the Dnp-albumins and the antibody was measured also by difference-spectral titrations at high protein concentrations. Antibody binding was increased under these conditions, but the Dnp group of mono-Dnp-albumin remained unavailable to antibody. We propose that the reactive lysine residues are located in clefts between the globular sub-domains of the single polypeptide chain. Dnp groups attached to these lysine residues are fully exposed to the solvent, but binding of the macromolecular probe, anti-Dnp antibody, is sterically hindered by the adjacent surface of the albumin molecule.

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.

scholarly journals Bovine serum albumin interactions with metal complexes

2014 ◽  
Vol 87 (4) ◽  
pp. 215-219 ◽  
Author(s):  
Tamara Topală ◽  
Andreea Bodoki ◽  
Luminiţa Oprean ◽  
Radu Oprean
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Complexes ◽  
Bovine Serum ◽  
Biological Functions ◽  
Pharmacokinetics And Pharmacodynamics ◽  
Serum Albumins ◽  
Pharmacological Agents ◽  
Drug Pharmacokinetics

The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral, antifungal and antineoplastic properties. As serum albumins play a key role in drug pharmacokinetics and pharmacodynamics, the study of coordination compounds affinity towards this class of proteins, as well as understanding the mechanism through which they interact is crucial. The aim of this review is to focus on the structure and biological functions of bovine serum albumin, the design of metal complexes that are able to bind to the biomolecule, as well as the experimental techniques employed in the study and evaluation of these interactions. Keywords: drug-protein interaction, coordination complex, fluorescence spectroscopy, UV-Vis absorption spectroscopy.

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