Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects

Jha, Niki S.; Kishore, Nand

doi:10.1016/j.tca.2008.10.012

Cited by 24 publications

(15 citation statements)

References 33 publications

(31 reference statements)

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“…3C). These C p values are similar to those found with other drugs binding to serum albumins, drug-DNA and protein-ligand interactions, and are generally attributed to burial of hydrophobic groups, the formation of a more compact drug-protein complex, and loss of water molecules due to binding [12,38,40,41].…”

Section: Heat Capacity Change and Enthalpy-entropy Compensationsupporting

confidence: 79%

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Bou-Abdallah

Sprague

Smith

et al. 2016

The Journal of Chemical Thermodynamics

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Serum albumins are ubiquitous proteins able to bind a variety of exogenous and endogenous ligands including hydrophobic pharmaceuticals. Most drugs bind to two very active binding regions located within sub-domains IIA and IIIA of the protein, also known as Sudlow's sites. The drug binding mode of serum albumin provides important pharmacological information and influences drug solubility, efficacy, biological distribution, and excretion. Here, the binding thermodynamics of Diclofenac and Naproxen, two non-steroidal anti-inflammatory drugs (NSAIDs) to bovine and human serum albumins (BSA and HSA, respectively) were studied by isothermal titration calorimetry (ITC), fluorescence spectroscopy and differential scanning calorimetry (DSC). The ITC data show that the binding affinity (K) of Diclofenac to BSA and HSA is on the order of 10 4 M-1 with a binding stoichiometry (n) of 2 drug molecules per protein. Naproxen binding to the two proteins exhibits a different profile with K and n values on the order of 10 6 M-1 and 0.75 for BSA and 10 5 M-1 and 3 for HSA, respectively. The binding of the two drugs to HSA is found to be both enthalpically and entropically favored suggesting the formation of hydrogen bonds and van der Waals hydrophobic effects. Binding of the two drugs to BSA is only enthalpically favored with an unfavorable entropy term. Significant enthalpyentropy compensation phenomena were reported for Diclofenac and Naproxen binding to BSA but not to HSA. Fluorescence quenching data between Diclofenac and the two proteins suggest static collisions and the formation of ground-state protein-drug complexes. The DSC data corroborate the ITC findings and show multiple sequential unfolding events and a strong drug stabilization effect at high drug to protein ratios. Overall, the calorimetric and spectroscopic data provided insights into the nature of these protein-drugs interactions and might offer useful information in future drug discovery studies.

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Section: Heat Capacity Change and Enthalpy-entropy Compensationsupporting

confidence: 79%

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Bou-Abdallah

Sprague

Smith

et al. 2016

The Journal of Chemical Thermodynamics

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“…Rather, the average lifetime has been utilized in order to receive a qualitative analysis. The average fluorescence lifetime reduces from 6.14 to 6.11 ns, at different chlorantraniliprole concentrations, suggesting formation of complex between chlorantraniliprole and HSA [36,37]. This result also coincides with previous discussion based on fluorescence emission that the quenching is static in nature.…”

Section: Time-resolved Fluorescencesupporting

confidence: 90%

Complexation of insecticide chlorantraniliprole with human serum albumin: Biophysical aspects

Ding

Liu

Diao

et al. 2011

Journal of Luminescence

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“…Quenching of BSA (2.5×10 −6 M) fluorescence emission intensity by ECG (1×10 −5 M) was followed in presence of 1 M sucrose; known for formation of hydrogen bonds through its hydroxyl groups [28]. The Stern-Volmer quenching constant (K SV ) was measured to be 1.9×10 5 M −1 which is more than an order less than that observed in absence of sucrose (Table 2).…”

Section: Resultsmentioning

confidence: 94%

Influence of Galloyl Moiety in Interaction of Epicatechin with Bovine Serum Albumin: A Spectroscopic and Thermodynamic Characterization

Pal

Saha²,

Hossain³

et al. 2012

PLoS ONE

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The health benefits stemming from green tea are well known, but the exact mechanism of its biological activity is not elucidated. Epicatechin (EC) and epicatechin gallate (ECG) are two dietary catechins ubiquitously present in green tea. Serum albumins functionally carry these catechins through the circulatory system and eliminate reactive oxygen species (ROS) induced injury. In the present study ECG is observed to have higher antioxidant activity; which is attributed to the presence of galloyl moiety. The binding affinity of these catechins to bovine serum albumin (BSA) will govern the efficacy of their biological activity. EC and ECG bind with BSA with binding constants 1.0×106 M−1 and 6.6×107 M−1, respectively. Changes in secondary structure of BSA on interaction with EC and ECG have been identified by circular dichroism (CD) and Fourier transform infrared (FT-IR) spectroscopy. Thermodynamic characterization reveals the binding process to be exothermic, spontaneous and entropy driven. Mixed binding forces (hydrophobic, electrostatic and hydrogen bonding) exist between ECG and BSA. Binding site for EC is primarily site-II in sub-domain IIIA of BSA and for ECG; it is site-I in sub-domain IIA. ECG with its high antioxidant activity accompanied by high affinity for BSA could be a model in drug designing.

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Binding of streptomycin with bovine serum albumin: Energetics and conformational aspects

Cited by 24 publications

References 33 publications

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Binding thermodynamics of Diclofenac and Naproxen with human and bovine serum albumins: A calorimetric and spectroscopic study

Complexation of insecticide chlorantraniliprole with human serum albumin: Biophysical aspects

Influence of Galloyl Moiety in Interaction of Epicatechin with Bovine Serum Albumin: A Spectroscopic and Thermodynamic Characterization

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