In vitro investigation of domain specific interactions of phenothiazine dye with serum proteins by spectroscopic and molecular docking approaches

Sharma, Arumugam Selva; Anandakumar, Shanmugam; Ilanchelian, Malaichamy

doi:10.1039/c4ra04630g

Cited by 57 publications

(37 citation statements)

References 49 publications

(79 reference statements)

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“…The HSA CD spectrum consists of one negative dichroic band located in the far UV spectral region, which is characteristic of the α-helical structure of the protein. 56 Ant-PIm , which is achiral, is thus CD inactive. 42 Upon addition of Ant-PIm to the HSA solution, a steady decrease in the negative ellipticities at 208 and 222 nm was observed indicating a decrease in the intrinsic HSA α-helix content ( Figure 5 ).…”

Section: Resultsmentioning

confidence: 99%

“…To provide quantitative information on the HSA secondary structure, we calculated the mean residue ellipticity (MRE) value at 208 nm and the α-helix % content using the following equations 56 where Θ 208 is the observed CD value (in millidegrees), C p is the concentration of the protein, l is the path length of the cuvette, and n is the number of amino acid residues of the protein (585); 4000 is the MRE of the β-sheet and random coil conformation at 208 nm and 33 000 is the MRE of a pure α-helix at 208 nm.…”

Section: Resultsmentioning

confidence: 99%

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Two-Photon Macromolecular Probe Based on a Quadrupolar Anthracenyl Scaffold for Sensitive Recognition of Serum Proteins under Simulated Physiological Conditions

et al. 2017

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The binding interaction of a biocompatible water-soluble polycationic two-photon fluorophore (Ant-PIm) toward human serum albumin (HSA) was thoroughly investigated under simulated physiological conditions using a combination of steady-state, time-resolved, and two-photon excited fluorescence techniques. The emission properties of both Ant-PIm and the fluorescent amino acid residues in HSA undergo remarkable changes upon complexation allowing the thermodynamic profile associated with Ant-PIm–HSA complexation to be accurately established. The marked increase in Ant-PIm fluorescence intensity and quantum yield in the proteinous environment seems to be the outcome of the attenuation of radiationless decay pathways resulting from motional restriction imposed on the fluorophore. Fluorescence resonance energy transfer and site-marker competitive experiments provide conclusive evidence that the binding of Ant-PIm preferentially occurs within the subdomain IIA. The pronounced hypsochromic effect and increased fluorescence enhancement upon association with HSA, compared to that of bovine serum albumin (BSA) and other biological interferents, makes the polymeric Ant-PIm probe a valuable sensing agent in rather complex biological environments, allowing facile discrimination between the closely related HSA and BSA. Furthermore, the strong two-photon absorption (TPA) with a maximum located at 820 nm along with a TPA cross section σ2 > 800 GM, and the marked changes in the position and intensity of the band upon complexation definitely make Ant-PIm a promising probe for two-photon excited fluorescence-based discrimination of HSA from BSA.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Two-Photon Macromolecular Probe Based on a Quadrupolar Anthracenyl Scaffold for Sensitive Recognition of Serum Proteins under Simulated Physiological Conditions

et al. 2017

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“…Therefore, the process of quenching the fluorescence of HSA interacting with EFHB is mediated primarily by a static mechanism. [4,5,[44][45][46] A Table 3. [47] The K a values for EFHB are 10 4 L mol -1 , suggesting very strong binding to HSA at the range of temperature studied.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods

Morales-Toyo

Glidewell

Bruno-Colmenares

et al. 2019

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Please cite this article as: M. Morales-Toyo, C. Glidewell, J. Bruno-Colmenares, et al., Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods, Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, https://doi. AbstractA novel hydrazone, (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate (EFHB), has been synthesized and characterized by FT-IR, NMR and Mass spectroscopy, and Xray diffraction; compound crystallized as translucent light yellow thin plates. EFHB was studied for their binding to human serum albumin (HSA) using the fluorescence quench titration method. Molecular docking was also performed to get a more detailed insight into their interaction with HSA at the binding site. Addition of this hydrazone to HSA ACCEPTED MANUSCRIPT A C C E P T E D M A N U S C R I P T2 produced significant fluorescence quenching and splitting of emission spectra of HSA through static quenching mechanism with binding constants of about 10 4 M -1 at 292. 15, 298.15, 304.15 and 310.15 K. According to the synchronous fluorescence, tryptophan and tyrosine residues of the protein are most perturbed by the binding process.Thermodynamic parameters ΔG, ΔH, and ΔS were got and the main sort of acting force between EFHB and HSA was studied. Results of molecular docking have shown that EFHB binds to subdomain IIA of HSA mainly by hydrophobic interaction, energy binding are in good agreement with those obtained by fluorescence study (ΔG the = -7.32 ± 0.09 kcal mol -1 and ΔG exp = -6.76 ± 0.03 kcal mol -1 ).

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“…The maximum uorescence intensity of TBZ decreased with the increase of DNA, indicating that the uorophore of TBZ was affected with the added DNA. The quenching constant (K sv ) and binding constant (K) were calculated by the linear Stern-Volmer equation 30,31 at four different temperatures (298, 303, 310, and 317 K) and were presented in Table 1. It is well-known that the decrease of K sv with the increased temperatures implies that the uorescence quenching mechanism is static quenching, whereas a reverse trend is dynamic quenching.…”

Section: The Normalized Affinity Indexes [A Nmentioning

confidence: 99%

Studies of the binding properties of the food preservative thiabendazole to DNA by computer simulations and NMR relaxation

Sun

Suo

et al. 2018

RSC Adv.

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In vitro investigation of domain specific interactions of phenothiazine dye with serum proteins by spectroscopic and molecular docking approaches

Abstract: In the present study the interaction of the chemotherapeutic agent, Azure A (AZA) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) was investigated by multi spectroscopic and molecular docking methods.

Cited by 57 publications

References 49 publications

Two-Photon Macromolecular Probe Based on a Quadrupolar Anthracenyl Scaffold for Sensitive Recognition of Serum Proteins under Simulated Physiological Conditions

Two-Photon Macromolecular Probe Based on a Quadrupolar Anthracenyl Scaffold for Sensitive Recognition of Serum Proteins under Simulated Physiological Conditions

Synthesis of (E)-Ethyl-4-(2-(furan-2-ylmethylene)hydrazinyl)benzoate, crystal structure, and studies of its interactions with human serum albumin by spectroscopic fluorescence and molecular docking methods

Studies of the binding properties of the food preservative thiabendazole to DNA by computer simulations and NMR relaxation

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