Hydrophobic Interactions in Proteins: Conformation Changes in Bovine Serum Albumin below pH 5*

Biochemistry ◽  
1964 ◽  
Vol 3 (9) ◽  
pp. 1377-1384 ◽  
Author(s):  
Arnold Wishnia ◽  
Thomas Pinder
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Conformation Changes

scholarly journals Hydrophobic interactions of phenoxazine modulators with bovine serum albumin

2000 ◽  
Vol 112 (1) ◽  
pp. 51-61 ◽  
Author(s):  
H. N. Kalpana ◽  
B. C. Channu ◽  
Chhabil Dass ◽  
P. J. Houghton ◽  
K. N. Thimmaiah
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydrophobic Interactions

Influence of Terahertz Radiation of Various Ranges on Molecule Conformation of Bovine Serum Albumin

2010 ◽  
Vol 5 (4) ◽  
pp. 182-185
Author(s):  
Angelina V. Kapralova ◽  
Aleksandr S. Pogodin
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Radiation Power ◽  
Uv Spectrophotometry ◽  
Absorption Bands ◽  
Conformation Changes ◽  
Protein Molecules ◽  
Molecule Conformation ◽  
Protein Bovine Serum Albumin

We investigated the influence of THz laser radiation of frequencies of 1.15 THz and 3.68 THz and radiation power of about 10 Mw on protein (bovine serum albumin). Using UV spectrophotometry, we revealed increase in the optical density of irradiated samples of bovine serum albumin at the characteristic absorption bands, which is evidence of conformation changes in protein molecules

Spectroscopic study of conformation changes of bovine serum albumin in aqueous environment

2019 ◽  
Vol 30 (6) ◽  
pp. 1302-1306 ◽  
Author(s):  
Chune Guo ◽  
Xiaomi Guo ◽  
Wubo Chu ◽  
Nan Jiang ◽  
He Li
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Spectroscopic Study ◽  
Bovine Serum ◽  
Aqueous Environment ◽  
Conformation Changes

scholarly journals Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling

2021 ◽  
Vol 22 (4) ◽  
pp. 1925
Author(s):  
Katarína Golianová ◽  
Samuel Havadej ◽  
Valéria Verebová ◽  
Jozef Uličný ◽  
Beáta Holečková ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Association Constants ◽  
Van Der Waals Interactions ◽  
Spectroscopic Methods ◽  
Spectroscopic Techniques ◽  
Conformation Changes

The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods.

scholarly journals The study on the interaction of Epigallocatechin gallate with bovine serum Albumin

2020 ◽  
pp. 1-9
Author(s):  
Gombosuren Davaadulam ◽  
Maamuu Tamara ◽  
Nyamaa Gerelsuren
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Epigallocatechin Gallate ◽  
Docking Simulation ◽  
Entropy Change ◽  
Ligand Docking ◽  
Number Of Binding Sites ◽  
Hoff Equation

In this study, we investigated the interaction of epigallocatechin gallate (EGCG) with bovine serum albumin (BSA) by fluorescence method and protein‐ligand docking. We separated EGCG from green tea using the chromatographic method and analyzed structural activity relationships of the EGCG. The results show that EGCG is a strong quencher of BSA fluorescence and binds with BSA with high affinity. The binding parameters (binding constant, the number of binding sites) were determined by the Ward equation. From the thermodynamic parameters, calculated according to the van’t Hoff equation, the enthalpy change ΔH°, and entropy change ΔS° were found to be -22.67 kJ/mol and 14.92 J/mol/K, respectively. These values suggest that apart from an initial hydrophobic association, the complex is held together by electrostatic and hydrogen bonding. In the docking simulation, the lowest free energies for the interaction of EGCG with tryptophan residues was −21.92kJ/mol (Trp134) and −24.7 kJ/mol (Trp213). The binding between EGCG and BSA consists of hydrogen bonds (Trp213) and hydrophobic interactions (Trp134).

Deciphering the binding patterns and conformation changes upon the bovine serum albumin–rosmarinic acid complex

2015 ◽  
Vol 6 (8) ◽  
pp. 2712-2726 ◽  
Author(s):  
Xin Peng ◽  
Xiangchao Wang ◽  
Wei Qi ◽  
Renliang Huang ◽  
Rongxin Su ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Rosmarinic Acid ◽  
Acid Complex ◽  
Conformation Changes ◽  
Naturally Occurring

Rosmarinic acid (RA) is an importantly and naturally occurring polyphenol. The interaction between bovine serum albumin and rosmarinic acid was studied to investigate the binding patterns and conformation changes.

Thermodynamics investigation of a series of metalloporphyrazine-bovine serum albumin complexes

2007 ◽  
Vol 11 (08) ◽  
pp. 556-565 ◽  
Author(s):  
A-Khalegh Bordbar ◽  
Hamid Dezhampanah ◽  
Mozaffar Asadi ◽  
Elham Safaei ◽  
Nasrin Sohrabi ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Fluorescence Emission ◽  
Resonance Light Scattering ◽  
Complex Model ◽  
Aggregate Formation ◽  
Fluorescence Studies ◽  
Induced Aggregation

The equilibrium binding of the tetra-cationic complexes ( N , N ′, N ″, N ‴-tetra-methyltetra-2,3-pyridinoporphyrazinato)copper(II), ([ Cu (2,3- TMTPPA )]4+), ( N , N ′, N ″, N ‴-tetra-methyltetra-3,4-pyridinoporphyrazinato)copper(II), ([ Cu (3,4- TMTPPA )]4+), (( N , N ′, N ″, N ‴-tetra-methyltetra-3,4-pyridinoporphyrazinato)cobalt(II), ([ Co (3,4- TMTPPA )]4+) and (( N , N ′, N ″, N ‴-tetra-methyltetra-3,4-pyridinoporphyrazinato)zinc(II), ([ Zn (3,4- TMTPPA )]4+) with bovine serum albumin (BSA) has been studied in phosphate buffer pH = 7.0 and at various temperatures using multi-spectroscopy techniques. The results of resonance light scattering (RLS) studies represent no aggregate formation of porphyrazine in the surface of BSA and low tendency of these porphyrazine for aggregate formation. The binding constants and binding stoichiometries were determined by analyzing of optical absorption spectra of porphyrazine complexes at various concentration of BSA using SQUAD software. The results show that the best fitting corresponds to a 1:1 complex model between BSA and porphyrazines. The thermodynamic parameters were calculated by van't Hoff equation at various temperatures. The data indicate that the process is entropy driven suggesting that hydrophobic interactions play a considerable role in the complex formation. The binding of porphyrazine complexes to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The average aggregation number of BSA, which has been calculated from the analysis of fluorescence quenching data, indicates the absence of any porphyrazine induced aggregation of BSA due to its interaction with porphyrazine complexes. Fluorescence studies also indicate that porphyrazine is bound to site I of BSA placed in sub-domain IIA, where tryptophan 214 is located.

scholarly journals Emissive Enhancement of the Singlet Oxygen Chemiluminescence Probe after Binding to Bovine Serum Albumin

Molecules ◽  
2019 ◽  
Vol 24 (13) ◽  
pp. 2422 ◽  
Author(s):  
Miranda-Apodaca ◽  
Hananya ◽  
Velázquez-Campoy ◽  
Shabat ◽  
Arellano
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Singlet Oxygen ◽  
Binding Sites ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Titration Calorimetry ◽  
Reaction Yield ◽  
Cell Penetrating Peptide ◽  
Thermal Stability Of

A chemiluminescence probe for singlet oxygen 1O2 (SOCL) was investigated in phosphate buffer saline (PBS), either in the absence of proteins or containing bovine serum albumin (BSA). In the protein-free PBS, the reactivity of SOCL for methylene blue (MB)-photosensitized 1O2 was found to be moderate or low. The reaction yield increased with temperature and/or concentration of dissolved molecular oxygen. Unexpectedly, the presence of BSA boosted both the emissive nature and the thermal stability of the phenoxy-dioxetane intermediate formed in the chemiexcitation pathway. Isothermal titration calorimetry showed that SOCL has a moderate binding affinity for BSA and that entropy forces drive the formation of the SOCL-BSA complex. A model with two identical and independent binding sites was used to fit the binding isotherm data. Co-operative binding was observed when MB was present. Local viscosity factors and/or conformational restrictions of the BSA-bound SOCL phenoxy-dioxetane were proposed to contribute to the formation of the highly emissive benzoate ester during the chemically initiated electron exchange luminescence (CIEEL) process. These results led us to conclude that hydrophobic interactions of the SOCL with proteins can modify the emissive nature of its phenoxy-dioxetane, which should be taken into account when using SOCL or its cell-penetrating peptide derivative in living cells.

The Investigation of the Interaction between Daidzin and Bovine Serum Albumin by Fluorescence Spectroscopy

2014 ◽  
Vol 664 ◽  
pp. 402-409
Author(s):  
Qing Ming Wang ◽  
Jia Liu ◽  
Tian Xing Zhang ◽  
Feng Zhu ◽  
Xin Hui Tang
Keyword(s):  
Bovine Serum Albumin ◽  
Hydrogen Bonds ◽  
Fluorescence Quenching ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Constant ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Binding Constants ◽  
Apparent Binding Constant

We investigated the mutual interaction of daidzin with bovine serum albumin (BSA) by fluorescence spectroscopy. The results revealed that daidzin cause the fluorescence quenching of BSA through a static quenching procedure. The Stern-Volmer quenching constant (Ksv) were calculated at different temperature. The binding site (n), apparent binding constant (Ka) and corresponding thermodynamic parameters △Go, △Ho, △Sowere calculated and the van der Waals interaction, hydrogen bonds and hydrophobic interactions play an important role in stabilizing the complex. Besides, we also studied the effect of Cu2+, Ni2+, Mn2+and Co2+on the binding constants between daidzin and BSA, it is shows that the binding of BSA and daidzin is strengthened in the presence metal ions.

scholarly journals Peculiarities of thermal aggregation of bovine serum albumin in the presence of strong polyelectrolytes

2020 ◽  
Vol 63 (9) ◽  
pp. 35-42
Author(s):  
Natalia N. Smirnova ◽  
◽  
Kirill V. Smirnov ◽  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Polymer Electrolyte ◽  
Sodium Salt ◽  
Bovine Serum ◽  
Temperature Increase ◽  
Hydrophobic Interactions ◽  
Maximum Yield ◽  
Maximum Output ◽  
Protein Molecules

The influence of temperature on bovine serum albumin (BSA) aggregation in aqueous solutions in the presence of poly-N,N-dimethyl-N,N-diallylammonium chloride (PDMDAAC) and the sodium salt of carboxymethylcellulose (CMC) was studied. It was shown that protein-polyelectrolyte complexes (PPC) form because of macromolecular reactions that are stabilized mainly by electrostatic forces. To characterize the PPC composition the φ parameter was used. This parameter is defined as the ratio of the concentration of ionic groups of polyelectrolyte per protein molecules. It was studied that when in an interpolyelectrolyte reaction, a sufficiently high degree of transformation occurs the polymer electrolyte initiates aggregation of protein molecules. As the temperature increases, the initiating role of the polymer electrolyte increases due to an increase in the intensity of hydrophobic interactions. Using the method of spectrophotometry, it was found that, depending on the nature of the polymer electrolyte, insoluble complexes of bovine serum albumin are formed when the pH parameter is above or below the isoelectric point of the protein, when its macromolecules are negatively or positively charged. In the presence of poly-N,N-dimethyl-N,N-diallylammonium chloride, the intensive formation of aggregates and their rapid precipitation in the form of flakes at pH > 7.0 was observed when the temperature increased to 60 °C. The maximum yield of the product of the interpolyelectrolyte reaction bovine serum albumin – sodium salt of carboxymethylcellulose was detected at pH ≤ 4.0. A temperature increase up to 60 °C, in this case, was not accompanied by intensive flocculation. Under optimal composition and interaction conditions, the degree of transformation in the BSA – PDMDAAX and BSA – CMC reactions is ~0.93 and 0.9, respectively, and decreases by ~5-7% with an increase in temperature to 60 °C. It was shown that for the same BOD composition (the ratio of components in the [CMC]/[BSA] complex = 0.1 g/g), an increase in temperature from 25 to 60 °C leads to the formation of particles that increase in size from 1 mcm to 5 mcm. The temperature increase leads to a change in composition of BOD, corresponding to its maximum output as a interpolyelectrolyte reactions product: for complex with PDMDAAC at T = 25, 40 and 60 °C, the φ value is 70, 60, 15; for the complex with the CMC – 60, 50, 20.

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