Thermodynamics and molecular bases of the interaction of ampicillin and streptomycin at their binding sites of bovine serum albumin

Kandeel, Mahmoud; Nakashima, Remi; Kitamura, Yoshiaki; Balaha, Mohamed; Abdel-Aziz, Magdy I.; Kitade, Yukio

doi:10.1007/s10973-012-2586-x

Cited by 5 publications

(2 citation statements)

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“…The main contribution to Δ G 0 is enthalpic. The negative Δ H for the binding of QUER to BSA at high as well as low affinity binding sites indicated that the binding process was exothermic and involved electrostatic interactions. , Furthermore, higher enthalpy change observed for the binding of QUER to the low affinity site indicates favorable placement of the hydrogen bond acceptor and donor groups at the binding interface …”

Section: Results and Discussionmentioning

confidence: 99%

Quercetin Influence on Thermal Denaturation of Bovine Serum Albumin

2016

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The effect of quercetin (QUER) binding on bovine serum albumin (BSA) thermal denaturation was systematically investigated by means of differential scanning calorimetry (DSC). Additional information concerning thermodynamic and structural binding parameters was provided by isothermal titration calorimetry (ITC) and molecular docking. The most relevant effect of QUER is manifested in the modification of the two-step thermal fingerprint of protein denaturation. Higher QUER concentrations result in a single-step denaturation thermogram, ascribed to the interplay between specific and nonspecific binding and enhancement of the solvent unfolding action. Analysis of ITC data indicate sequential binding of two molecules of QUER occurring spontaneously at different binding sites of BSA involving hydrophobic, electrostatic and hydrogen binding forces. Identification of QUER binding sites was possible through corroboration of DSC runs in the presence of site markers and molecular docking. Modeling of ligand-protein interaction confirmed the experimental data. On one hand, a neutral form of QUER binds in a nonplanar conformation to Sudlow's site I, a large hydrophobic cavity of subdomain IIA of BSA and decreases its thermal stability. On the other hand, a second molecule of QUER, the anionic form, is bound in planar conformation to Sudlow's site II, situated in the subdomain IIIA of the folded protein, and increases the thermal stability of the corresponding structural domain of the protein.

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Section: Results and Discussionmentioning

confidence: 99%

Quercetin Influence on Thermal Denaturation of Bovine Serum Albumin

2016

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“…Using ITC, Kandeel et al analyzed the binding of streptomycin to BSA. This antibiotic showed very low binding affinity for BSA (the K a value of the order between 10 4 and 10 3 M −1 ) and the number of binding sites on the BSA surface (stoichiometry/N) has been identified as 11 ± 0.7 [ 42 ]. On the other hand, Scholtan et al estimated the K a and the n parameter for the binding of streptomycin with HSA equaled 3 × 10 2 M −1 and about 17, respectively [ 43 ].…”

Section: Discussionmentioning

confidence: 99%

The effect of selected aminoglycoside antibiotics on human serum albumin antioxidant activity: a spectroscopic and calorimetric comparative study

Rogóż,

Mac,

Owczarzy

et al. 2023

Pharmacol. Rep

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Background Human serum albumin (HSA) is a valuable component of non-enzymatic and endogenous antioxidant mechanisms. The antioxidant activity of HSA can be modulated by ligands, including drugs. Although this is a central topic in the field of oxidation, there is still a lack of information about the protection against the effects of elevated free radical levels. Methods The aim of this study was to investigate the antioxidant activity of kanamycin (KAN) and neomycin (NEO) and their effect on the antioxidant potential of HSA using spectroscopic and microcalorimetric techniques. Results Despite the fact that kanamycin and neomycin interact with HSA, no changes in the secondary structure of the protein have been observed. The analysis of the aminoglycoside antibiotics showed their low antioxidant activity and a synergistic effect of the interaction, probably due to the influence of ligands (KAN, NEO) on the availability of HSA amino acid residues functional groups, such as the free thiol group (Cys-34). Conclusions Based on the spectroscopic and microcalorimetric data, both KAN and NEO can be considered modulators of the HSA antioxidant activity.

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