Evidence of two structurally related solvatochromic probes complexed with β-cyclodextrin by using spectroscopic methods

Ghosh, Sujay; Mitra, Amrit Krishna; Pal, Uttam; Basu, Samita; Saha, Chandan

doi:10.1016/j.molstruc.2016.10.097

Cited by 11 publications

(7 citation statements)

References 56 publications

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“…With the continuous addition of 9-OHPhe, regular quenching of HSA fluorescence was observed, indicating that an obvious interaction occurred between HSA and 9-OHPhe. Moreover, an isosbestic point was observed at around 358.0 nm in the HSA-9-OHPhe system, which suggested that the interaction between HSA and 9-OHPhe reached equilibrium. , …”

Section: Resultsmentioning

confidence: 90%

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Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study

et al. 2020

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9-Hydroxyphenanthrene (9-OHPhe), the representative hydroxyl metabolite of phenanthrene, has generated increasing concern as it is potentially hazardous to organisms. Herein, multispectroscopic and molecular docking techniques were applied to investigate the molecular interaction of human serum albumin (HSA) with 9-hydroxyphenanthrene (9-OHPhe) under simulated physiological conditions. Steady-state fluorescence and time-resolved fluorescence spectral analysis showed that 9-OHPhe quenched HSA fluorescence through a mixed static and dynamic process. HSA can bind with 9-OHPhe to form a 1:1 complex, with binding constants of 1.28 × 10 5 , 1.36 × 10 5 , and 1.26 × 10 5 L·mol –1 at 298.15, 303.15, and 308.15 K, respectively. The strong binding between HSA and 9-OHPhe is spontaneous and entropy-driven. Molecular docking indicated that the optimal binding site of 9-OHPhe with HSA was located in the IA subdomain of HSA. Thermodynamic analysis and molecular docking results suggested that hydrophobic interactions and hydrogen bond force dominated the binding process of HSA with 9-OHPhe. Specifically, 9-OHPhe formed hydrophobic interactions with LEU134, LEU139, ILE142, LEU154, PHE157, ALA158, and TYR161 and formed a 1.86 Å hydrogen bond with LEU135. Circular dichroism spectral analysis showed that the α-helical content of HSA decreased from 52.3 to 50.9% after adding 9-OHPhe with a ratio of 1:1. The obtained results are hoped to provide basic data for understanding the potential effects of the hydroxyl metabolites of PAHs on functional biomacromolecules.

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Section: Resultsmentioning

confidence: 90%

“…Moreover, an isosbestic point was observed at around 358.0 nm in the HSA-9-OHPhe system, which suggested that the interaction between HSA and 9-OHPhe reached equilibrium. 27,28 3.2. Fluorescence Quenching Mechanism of the HSA-9-OHPhe System.…”

Section: Resultsmentioning

confidence: 99%

Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study

et al. 2020

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“…As Erlo concentration gradually increases, quenching of the protein's inherent fluorescence is observed, confirming that Erlo interacted with HSA. After the interaction with Erlo, an isosbestic point appears at ~369 nm, which indicates an equilibrium in the drug–protein interaction process [24, 25]. During the drug–protein interaction process, the maximum wavelength is slightly shifted toward shorter wavelengths (from 345 to 333 nm), indicating a decrease in the polarity of the environment around tryptophan [26].…”

Section: Resultsmentioning

confidence: 99%

Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

et al. 2023

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Human serum albumin (HSA) is a globular and monomeric protein in plasma that transports many drugs and compounds. Binding of some drugs to HSA can lead to changes in its stability and biological function. We investigated the binding interactions between erlotinib hydrochloride (Erlo) and HSA. Erlo is used to treat lung, pancreatic, and some other cancers. Experimental data showed that the fluorescence emission of the protein was quenched by Erlo using a static quenching mechanism. The calculation of the binding constant, K b (1.57 Â 10 5 M À1 at 300 K), confirmed the existence of a moderate binding interaction between Erlo and HSA.The interaction was enthalpy driven, spontaneous, and exothermic. The calculated thermodynamic parameters in agreement with simulation and molecular docking data showed that van der Waals and hydrogen bond forces played an important role in the interaction process. Molecular docking results indicated that Erlo has more affinity to bind to subdomain IIA (site I) of HSA. Molecular dynamics simulation analysis showed that the protein is stable in the presence of Erlo under simulation conditions.

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“…We have seen the importance of organised assemblies on biological and photophysical processes over the last three decades [ 131 , 133 , 146 – 149 ]. Because of their applications in assorted biophysical and biochemical processes, there has been a developing interest in the study of various photoprocesses occurring in electronically excited molecules in various organised microheterogeneous environments such as micelles, reverse micelles, cyclodextrins and so on [ 146 – 149 ].…”

Section: Application Of Phenoxazine As Fluorescent Probesmentioning

confidence: 99%

Synthetic, biological and optoelectronic properties of phenoxazine and its derivatives: a state of the art review

Sadhu¹,

Mitra²

2023

Mol Divers

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Phenoxazines have sparked a lot of interest owing to their numerous applications in material science, organic light-emitting diodes, photoredox catalyst, dye-sensitized solar cells and chemotherapy. Among other things, they have antioxidant, antidiabetic, antimalarial, anti-alzheimer, antiviral, anti-inflammatory and antibiotic properties. Actinomycin D, which contains a phenoxazine moiety, functions both as an antibiotic and anticancer agent. Several research groups have worked on various structural modifications over the years in order to develop new phenoxazines with improved properties. Both phenothiazines and phenoxazines have gained prominence in medicine as pharmacological lead structures from their traditional uses as dyes and pigments. Organoelectronics and material sciences have recently found these compounds and their derivatives to be quite useful. Due to this, organic synthesis has been used in an unprecedented amount of exploratory alteration of the parent structures in an effort to create novel derivatives with enhanced biological and material capabilities. As a result, it is critical to conduct more frequent reviews of the work done in this area. Various stages of the synthetic transformation of phenoxazine scaffolds have been depicted in this article. This article aims to provide a state of the art review for the better understanding of the phenoxazine derivatives highlighting the progress and prospects of the same in medicinal and material applications. Graphical abstract

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Evidence of two structurally related solvatochromic probes complexed with β-cyclodextrin by using spectroscopic methods

Cited by 11 publications

References 56 publications

Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study

Probing the Interaction between Human Serum Albumin and 9-Hydroxyphenanthrene: A Spectroscopic and Molecular Docking Study

Probing the combination of erlotinib hydrochloride, an anticancer drug, and human serum albumin: Spectroscopic, molecular docking, and molecular dynamic analyses

Synthetic, biological and optoelectronic properties of phenoxazine and its derivatives: a state of the art review

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