Investigation of binding behaviour of procainamide hydrochloride with human serum albumin using synchronous, 3D fluorescence and circular dichroism

Byadagi, Kirthi S.; Meti, Manjunath D.; Nandibewoor, Sharanappa T.; Chimatadar, Shivamurti A.

doi:10.1016/j.jpha.2016.07.004

Cited by 44 publications

(12 citation statements)

References 35 publications

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“…Synchronous fluorescence spectroscopy is a sensitive method used to probe changes in the binding pocket conformation and polarity upon ligand binding to a protein [ 24 ]. Often, ligand-induced protein conformational changes lead to binding pocket realignment which can affect the microenvironment of nearby HSA’s fluorophores, Trp (214) and Tyr (150, 411, 452) residues.…”

Section: Resultsmentioning

confidence: 99%

Binding Studies of AICAR and Human Serum Albumin by Spectroscopic, Theoretical, and Computational Methodologies

et al. 2020

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The interactions of small molecule drugs with plasma serum albumin are important because of the influence of such interactions on the pharmacokinetics of these therapeutic agents. 5-Aminoimidazole-4-carboxamide ribonucleoside (AICAR) is one such drug candidate that has recently gained attention for its promising clinical applications as an anti-cancer agent. This study sheds light upon key aspects of AICAR’s pharmacokinetics, which are not well understood. We performed in-depth experimental and computational binding analyses of AICAR with human serum albumin (HSA) under simulated biochemical conditions, using ligand-dependent fluorescence sensitivity of HSA. This allowed us to characterize the strength and modes of binding, mechanism of fluorescence quenching, validation of FRET, and intermolecular interactions for the AICAR–HSA complexes. We determined that AICAR and HSA form two stable low-energy complexes, leading to conformational changes and quenching of protein fluorescence. Stern–Volmer analysis of the fluorescence data also revealed a collision-independent static mechanism for fluorescence quenching upon formation of the AICAR–HSA complex. Ligand-competitive displacement experiments, using known site-specific ligands for HSA’s binding sites (I, II, and III) suggest that AICAR is capable of binding to both HSA site I (warfarin binding site, subdomain IIA) and site II (flufenamic acid binding site, subdomain IIIA). Computational molecular docking experiments corroborated these site-competitive experiments, revealing key hydrogen bonding interactions involved in stabilization of both AICAR–HSA complexes, reaffirming that AICAR binds to both site I and site II.

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Section: Resultsmentioning

confidence: 99%

Binding Studies of AICAR and Human Serum Albumin by Spectroscopic, Theoretical, and Computational Methodologies

et al. 2020

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“…This in turn prohibited AMI binding with BSA and reduced the AMI storage time in plasma followed by a rapid clearance from the body. [ 48,50 ] The number of binding sites for AMI in the presence of all metal ions (copper, ferrous, zinc, lead ) was approximately one.…”

Section: Resultsmentioning

confidence: 99%

Effect of quercetin on the amiloride–bovine serum albumin interaction using spectroscopic methods, molecular docking and chemometric approaches

et al. 2020

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The effect of quercetin flavonoid (QUE), on the binding interaction of antihypertensive drug, amiloride (AMI) with bovine serum albumin (BSA) was investigated in this study. Spectroscopic methods such as steady‐state, synchronous, three‐dimensional fluorescence, and circular dichroism spectroscopy were employed to study the interaction. Fluorescence data were analyzed using the Stern–Volmer equation and a static quenching process was found to be involved in the formation of AMI–BSA and QUE–BSA complexes and were in good agreement with the thermodynamic study. The thermodynamic parameters illustrated that the process is spontaneous and enthalpy driven. Hydrophobicity is acting as the primary force in the binding interaction. Fluorescence spectral data were resolved using a multivariate curve resolution‐alternating least squares method (MCR–ALS). Site marker and molecular docking studies confirmed the binding site of AMI on BSA, i.e. site II. The binding distance between amino acid of BSA and AMI was calculated and found to be 2.18 nm which indicated that energy transfer has occurred from an amino acid of BSA to AMI. The binding affinity of AMI to BSA was found to be reduced in the presence of QUE, which may lead to the poor distribution of AMI at the desired site.

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“…53 On the other hand, when Dλ = 60 nm, the addition of NQA, NQC, and NQF to the albumin solution led to a slight red shift of the HSA signal (from 280 to 283; 288; and 288 nm for NQA, NQC, and NQF, respectively), indicating that they can perturb the microenvironment around the Trp-214 residue by increasing the polarity around this main albumin fluorophore. 54,55 Competitive binding studies and molecular docking analysis…”

Section: Samplementioning

confidence: 99%

Antibacterial Activity of 2-Amino-1,4-naphthoquinone Derivatives Against Gram‑Positive and Gram-Negative Bacterial Strains and Their Interaction with Human Serum Albumin

Silva

Chaves

Paiva

et al. 2020

J. Braz. Chem. Soc.

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A series of 2-amino-1,4-naphthoquinone derivatives (NQA-NQF) was synthesized by alternative methods (ultrasonication and microwave irradiation), with yields ranging from 40 to 71%, and without the need of further recrystallization. Each compound was evaluated against four Gram-positive (Bacillus subtilis, Enterococcus faecalis, Staphylococcus aureus and Bacillus cereus) and five Gram-negative (Escherichia coli, Klebsiella pneumoniae, Pseudomonas aeruginosa, Acinetobacter baumannii and Klebsiella pneumoniae positive β-lactamase) bacteria strains. The NQF was the most active amino-naphthoquinone derivative with minimum inhibitory concentration (MIC) of 31.2 µg mL-1 against K. pneumoniae positive β-lactamase (a common intestinal bacteria which can cause life-threatening infections). On the other hand, NQA and NQC showed good activity as a potential antibiotic for the bacteria strains assayed, except for K. pneumoniae. In addition, the affinity of these three most active compounds (NQA, NQC, and NQF) for human serum albumin (HSA) was evaluated employing multiple spectroscopic techniques (steady-state, time-resolved, and synchronous fluorescence, as well as circular dichroism), combined with theoretical calculations (molecular docking). The interaction HSA:2-amino-1,4-naphthoquinones occurs spontaneously and moderately inside the subdomain IIA (Sudlow's site I) via hydrogen bonding and van der Waals forces.

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Investigation of binding behaviour of procainamide hydrochloride with human serum albumin using synchronous, 3D fluorescence and circular dichroism

Cited by 44 publications

References 35 publications

Binding Studies of AICAR and Human Serum Albumin by Spectroscopic, Theoretical, and Computational Methodologies

Binding Studies of AICAR and Human Serum Albumin by Spectroscopic, Theoretical, and Computational Methodologies

Effect of quercetin on the amiloride–bovine serum albumin interaction using spectroscopic methods, molecular docking and chemometric approaches

Antibacterial Activity of 2-Amino-1,4-naphthoquinone Derivatives Against Gram‑Positive and Gram-Negative Bacterial Strains and Their Interaction with Human Serum Albumin

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