Spectroscopic and Molecular Modeling Studies on Binding of Sparfloxacin to Humain Serum Albumin

2012 ◽  
Vol 518-523 ◽  
pp. 494-497
Author(s):  
Cheng Yu Dong ◽  
Ying Liu
Keyword(s):  
Molecular Modeling ◽  
Serum Albumin ◽  
Binding Sites ◽  
Specific Binding ◽  
Inner Filter Effect ◽  
Binding Parameters ◽  
Modeling Methods ◽  
Specific Binding Sites ◽  
Molecular Modeling Studies ◽  
Site Marker

The interaction between sparfloxacin (SPFX) and human serum albumin (HSA) had been studied by spectroscopic and molecular modeling methods. The inner filter effect was eliminated to get accurate binding parameters. The site marker competition experiments revealed that SPFX binds to site I (subdomain IIA) of HSA and molecular docking was employed to further define the specific binding sites.

THE BINDING OF ETHACRYNIC ACID TO BOVINE SERUM ALBUMIN

1967 ◽  
Vol 45 (9) ◽  
pp. 1433-1443 ◽  
Author(s):  
Edward Ronwin ◽  
Anthony G. Zacchei
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Plasma Protein ◽  
Binding Sites ◽  
Bovine Serum ◽  
Concentration Ratio ◽  
Ethacrynic Acid ◽  
Specific Binding ◽  
Albumin Fraction ◽  
Specific Binding Sites

Studies with 14C-labelled ethacrynic acid indicated that this potent diuretic binds to the albumin fraction of plasma protein. An investigation of the variation of molar binding as a function of the molar concentration ratio revealed that a mole of bovine serum albumin can bind 4 moles of ethacrynic acid strongly (probably irreversibly) and approximately 12 moles reversibly at pH 7.4. Further, it appears that the protein could accommodate a maximum of approximately 16 reversibly bound moles of ethacrynic acid at this pH. Efforts to determine the chemical identity of specific binding sites did not allow positive assignments.

Spectral investigations of the interaction of some porphyrins with bovine serum albumin

2000 ◽  
Vol 04 (02) ◽  
pp. 147-157 ◽  
Author(s):  
SHAMPA CHATTERJEE ◽  
T. S. SRIVASTAVA
Keyword(s):  
Energy Transfer ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Binding Sites ◽  
Bovine Serum ◽  
Tertiary Structure ◽  
Specific Binding ◽  
Specific Binding Sites ◽  
Cd Studies

The binding of meso-tetrakis[4-(carboxymethyleneoxy)phenyl]porphyrin (T4CPP), meso-tetrakis[3-(carboxymethyleneoxy)phenyl]porphyrin (T3CPP) and meso-tetrakis[3,4-bis(carboxymethyl-eneoxy)phenyl]porphyrin (T3, 4BCPP) with bovine serum albumin (BSA) at pH 7.4 has been studied at 420 nm in detail. The results show hypochromicity along with a red shift in the Soret band of the porphyrins. This suggests that these porphyrins bind to BSA as monomers. Further analysis of these data supports the non-interactive binding of T4CPP and T3CPP with BSA and the cooperative binding of T3, 4BCPP with BSA. These binding data have been interpreted in terms of one specific binding site and several non-specific binding sites on BSA for the porphyrins. The absorption spectral changes of the porphyrins between 400 and 450 nm when titrated with BSA suggest that there is another specific binding site on BSA for the porphyrins. These two specific binding sites have also been supported by circular dichroism (CD) studies. The absorption spectral and CD studies on the interactions of the porphyrins with BSA further suggest that these interactions are dependent on the number and configuration of substituents in the phenyl groups of the porphyrins. The contact energy transfer from the aromatic amino acid residues tryptophan and tyrosine of BSA to the porphyrins in the BSA–porphyrin complexes has also been studied using fluorescence spectroscopy. These energy transfer data show the energy transfer from tryptophan to the porphyrins for their binding to site I of BSA and from tyrosine to the porphyrins for their binding to site II of BSA. Unfolding studies of the BSA–porphyrin systems indicate that the tertiary structure is essential for the binding of the porphyrins. A correlation between the accumulation of99 mTc -labelled T4CPP and T3, 4BCPP in tumour tissue and their binding at site II of BSA is possible. The interaction of the porphyrins can also be used as a model for mitochondrial interactions.

Recreational drugs 25I-NBOH and 25I-NBOMe bind to both Sudlow's sites I and II of Human Serum Albumin (HSA): Biophysical and molecular modeling studies

2021 ◽  
Author(s):  
Wellington Alves de Barros ◽  
Marina de Magalhães Silva ◽  
Maria Dayanne de Araújo Dantas ◽  
Josue Santos ◽  
Isis Figueiredo ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Modelling ◽  
Recreational Drugs ◽  
Modeling Studies ◽  
Molecular Modelling Studies ◽  
Modelling Studies ◽  
Molecular Modeling Studies

Experimental, biophysical, and molecular modelling studies between 25I-NBOH and 25I-NBOMe with human serum albumin (HSA) have indicated that these recreational drugs simultaneously bind to site I and II of the...

scholarly journals Specific Binding of Rubidium in Chlorella

1962 ◽  
Vol 45 (5) ◽  
pp. 959-977 ◽  
Author(s):  
Dan Cohen
Keyword(s):  
Active Transport ◽  
Binding Sites ◽  
Specific Binding ◽  
High Concentration ◽  
External Concentration ◽  
Specific Binding Sites ◽  
Dense Suspension ◽  
Concentration Of Ions ◽  
The Individual ◽  
A Site

Specific binding sites for potassium, which may be components of the carriers for active transport for K in Chlorella, were characterized by their capacity to bind rubidium. A dense suspension was allowed to take up Rb86 from a low concentration of Rb86 and a high concentration of ions which saturate non-specific sites. The amount bound was derived from the increase in the external concentration of Rb86 following addition of excess potassium. The sites were heterogeneous. The average affinity of Rb and various other ions for the sites was determined by plotting the degree of displacement of Rb86 against log molar concentration of the individual ions. Interpolation gave the concentration for 50 per cent displacement of Rb, which is inversely related to affinity. The order of affinity was not changed when the cells were frozen, or boiled either in water or in 70 per cent ethanol. The affinity is maximal for ions with a crystalline radius of 1.3 to 1.5 A and a high polarizability, and is not related to the hydrated radius or valency. It is suggested that binding groups in a site are rigidly arranged, the irregular space between them being 2.6 to 3.0 A across, so that affinity is high for ions of this diameter and high polarizability.

Studies of the uptake of macromolecules by cells. I. Uptake of proteins by cells of the Ehrlich–Lettré ascites carcinoma

1968 ◽  
Vol 46 (12) ◽  
pp. 1443-1450 ◽  
Author(s):  
Y. C. Choi ◽  
E. R. M. Kay
Keyword(s):  
Nucleic Acid ◽  
Cell Membrane ◽  
Binding Sites ◽  
Specific Binding ◽  
Protein Uptake ◽  
Specific Binding Sites ◽  
Model Protein ◽  
Uptake Process ◽  
Kinetics Of ◽  
Protein Treatment

The uptake of protein by cells of the Ehrlich–Lettré ascites carcinoma was characterized kinetically by using hemoglobin as a model protein. An attempt was made to show that the process is not an artefact due to nonspecific adsorption of protein to the cell membrane. The kinetics of the uptake process suggested that an interaction exists between the exogenous protein and specific binding sites on the membrane. Acetylation of hemoglobin enhanced the rate of uptake of this protein. Treatment of cells with neuraminidase, phospholipase A, and Pronase resulted in an inhibition of protein uptake. The experimental evidence for the uptake of hemoglobin was supported by evidence that L-serine-U-14C-labelled hemoglobin is transported into the cytoplasm and utilized subsequently, resulting in labelling of the nucleic acid nucleotides.

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