Investigation on intermolecular interaction of synthesized azo dyes with bovine serum albumin

Dezhampanah, Hamid; Mohammadi, Asadollah; Pour, Amineh Mousazadeh Moghaddam

doi:10.1080/07391102.2021.2015444

Cited by 8 publications

(2 citation statements)

References 27 publications

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“…A reliable and versatile method for characterizing interactions and gaining access to the surroundings of fluorophores in the protein matrix is fluorescence spectroscopy . Phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) are major amino acid residues responsible for the intrinsic fluorescence of the protein and are very sensitive toward their microenvironment. − BSA has 583 amino acids, out of which 20 are tyrosyl and 2 are tryptophan residues . Therefore, in order to obtain mechanistic insights into the mode of the dye–protein interaction, fluorescence spectroscopy was employed.…”

Section: Resultsmentioning

confidence: 99%

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Jain,

Judy,

Kishore

2024

J. Phys. Chem. B

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Many studies have demonstrated the manner in which ANS interacts with bovine serum albumin (BSA), although they are limited by the extremely low solubility of dye. The present study demonstrates the binding of ANSA dye with BSA, and since this dye can easily replace ANS, it not only simplifies research but also improves sensor accuracy for serum albumin. A combination of calorimetry and spectroscopy has been employed to establish the thermodynamic signatures associated with the interaction of ANSA with the protein and the consequent conformational changes in the latter. The results of differential scanning calorimetry reveal that when the concentration of ANSA in solution is increased, the thermal stability of the protein increases substantially. The fluorescence data demonstrated a decrease in the binding affinity of ANSA with the protein when pH increased but was unable to identify a change in the mode of interaction of the ligand. ITC has demonstrated that the mode of interaction between ANSA and the protein varies from a single set of binding sites at pH 5 and 7.4 to a sequential binding site at pH 10, emphasizing the potential relevance of protein conformational changes. TCSPC experiments suggested a dynamic type in the presence of ANSA. Molecular docking studies suggest that ANSA molecules are able to find ionic centers in the hydrophobic pockets of BSA. The findings further imply that given its ease of use in experiments, ANSA may be a useful probe for tracking the presence of serum albumin and partially folded protein states.

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Section: Resultsmentioning

confidence: 99%

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Jain,

Judy,

Kishore

2024

J. Phys. Chem. B

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“…Employing fluorescence techniques, we have illustrated the role and governance of BSA in the ground and excited state properties of AD dyes , such that the dye molecule prefers to reside in a multiheterogeneous microenvironment (buried or exposed) comprising hydrophilic and hydrophobic phases. Further, spectroscopic techniques assisted by electrochemical and theoretical studies have imparted a crucial role in establishing the nature of interactions of several dyes with BSA. − Molecular docking (Mol.Doc) studies authenticate the binding domains and most preferred site of dye/drug in the protein structure. The combined theoretical and experimental approach provides substantial information on the nature of interactions in several studies involving ligands (dye or drug), which is of larger significance in the concept of biophysical chemistry at the molecular level.…”

Section: Introductionmentioning

confidence: 99%

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

et al. 2023

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Molecular docking (Mol.Doc) techniques were employed to ascertain the binding affinity of two resorcinol-based acridinedione dyes (ADR1 and ADR2) with the widely studied globular protein Bovine Serum Albumin (BSA) in the presence of site-selective binding drugs by Autodock Vina 4.2 software. Docking of various feasible conformers of ADR1 dye with BSA was found to be energetically more favored than ADR2 dye, even though both these dyes differ in the 9th position of the basic dye structure. Analysis of dyes with BSA establishes the location of dye in all of the binding sites of BSA, predominantly through conventional and nonconventional hydrogen-bonding (HB) interactions. The coexistence of hydrophobic interactions resulted in the stability of various conformers generated. The introduction of site I and site II (Sudlow site binding drugs) into ADR1−BSA and ADR2−BSA complexes effectively destabilizes the dye−protein complex; however, the drugs do not displace ADR dyes completely from their selective binding domains. Site II binding drugs effectively destabilize the binding ability of the dye−protein complex rather than site I drugs. However, docking of site I drug 3-carboxyl-4-methyl-5-propyl-2-furanpropanic acid (CMPF) largely destabilizes the ADR1−protein complex, whereas indomethacin (INDO) enhances the binding affinity of the ADR2−protein complex. Interestingly, simultaneous docking of ADR dyes to the BSA−drug complex results in larger stability of the protein−drug complex through HB interactions rather than hydrophobic interactions. Both ADR1 and ADR2 dyes predominantly occupy the Sudlow binding sites of BSA, and the introduction of either site I or site II binding drugs does not displace the dye efficiently from the corresponding binding sites, rather the drugs are effectively displaced toward other binding domains apart from their specific site-binding domains of BSA. Through Mol.Doc techniques, we authenticate that the interactions in host−guest complex systems involving competing ligands are established in depth, wherein the dye as well as the amino acid (AA) moieties in BSA act as both HB donor and acceptor sites apart from several hydrophobic interactions coexisting toward the stability.

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Investigating the Serum Albumin Binding Behavior of Naphthalimide Based Fluorophore Conjugates: Spectroscopic and Molecular Docking Approach

Gupta,

Paul

2024

ChemMedChem

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In the present study, naphthalimide‐pyrazole‐benzothiazole based fluorescent analogs were synthesized by substituting different primary and secondary amines on the naphthalimide nucleus and were evaluated for their sensitivity and selectivity towards serum albumin. Among various synthesized analogues compound 25 showed the most significant change with serum albumin and was further studied for selective detection and mode of interaction with serum albumin. Here, we compared the binding interaction of fluorescent probe 25 for variation/detection of two 76% structurally resembling proteins HSA and BSA, by spectroscopic experiments. The compound shows more selectivity for HSA and BSA with a higher binding constant and evident visible change in the emission spectra of two serum albumins among different bioanalytes. The mode of interaction of 25 with human serum albumin and bovine serum albumin was investigated by FT‐IR, circular dichroism, and DLS techniques to find out the change in the microenvironment and variation in the structure of serum albumin proteins. Higher binding affinity and specific selectivity of 25 with a limit of detection of 0.69 µM and 1.4 µM towards HSA and BSA compared to other bioanalytes make it a significant fluorescent probe for quantitatively detecting serum albumins at the very early stage of many fatal diseases.

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Investigation on intermolecular interaction of synthesized azo dyes with bovine serum albumin

Cited by 8 publications

References 27 publications

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Analytical Aspects of ANSA–BSA Association: A Thermodynamic and Conformational Approach

Complexity of the Role of Various Site-Specific and Selective Sudlow Binding Site Drugs in the Energetics and Stability of the Acridinedione Dye–Bovine Serum Albumin Complex: A Molecular Docking Approach

Investigating the Serum Albumin Binding Behavior of Naphthalimide Based Fluorophore Conjugates: Spectroscopic and Molecular Docking Approach

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