Synthesis, Photophysical Properties, <i>in Vivo</i> Photosensitizing Efficacy, and Human Serum Albumin Binding Properties of Some Novel Bacteriochlorins

Pandey, Ravindra K.; Constantine, Scott; Tsuchida, Takaaki; Zheng, Gang; Medforth, Craig J.; Aoudia, Mohamed; Kozyrev, Andrei N.; Rodgers, Michael A. J.; Kato, Harubumi; Smith, Kevin M.; Dougherty, Thomas J.

doi:10.1021/jm9702894

Cited by 93 publications

(73 citation statements)

References 32 publications

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“…It has been shown that DA and DP are two fluorescence probes, which are specific, respectively, for the two drug binding sites on HSA (Pandey et al 1997;Jisha et al 2006). In their free form, the two probes emit negligible fluorescence.…”

Section: Tryptophan Intrinsic Fluorescencementioning

confidence: 99%

Fluorescence study on site-specific binding of perfluoroalkyl acids to human serum albumin

2008

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Binding of five perfluoroalkyl acids with human serum albumin (HSA) was investigated by sitespecific fluorescence. Intrinsic fluorescence of tryptophan-214 in HSA was monitored upon addition of the chemicals. Although perfluorobutyl acid (PFBA) and perfluorobutane sulfonate (PFBS) did not cause fluorescence change, perfluorooctanoic acid (PFOA), perfluorooctane sulfonate (PFOS), and perfluorododecanoic acid (PFDoA) induced fluorescence quenching, from which binding constant of 2.7 9 10 5 M -1 for PFOA and 2.2 9 10 4 M -1 for PFOS was calculated. Two fluorescent probes, dansylamide (DA) and dansyl-L-proline (DP), were employed in fluorescence displacement measurements to study the interaction at two Sudlow's binding sites. At Site I, both PFBA and PFBS displaced DA with binding constants of 1.0 9 10 6 M -1 and 2.2 9 10 6 M -1 . At Site II, PFBS and PFDoA displaced DP with binding constants of 6.5 9 10 6 M -1 and 1.2 9 10 6 M -1 , whereas PFBA did not bind. The data were compared with fatty acids to evaluate the potential toxicological effect of these environmental chemicals.

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Section: Tryptophan Intrinsic Fluorescencementioning

confidence: 99%

Fluorescence study on site-specific binding of perfluoroalkyl acids to human serum albumin

2008

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“…Serum albumin is the major protein constituent of blood plasma. Specifi c delivery of ligands by BSA is considered to be due to the presence of two selective binding sites, namely site I and site II [55]. Dansyl amides are known to bind with site I through hydrophobic interactions [55].…”

Section: (B)mentioning

confidence: 99%

“…Specifi c delivery of ligands by BSA is considered to be due to the presence of two selective binding sites, namely site I and site II [55]. Dansyl amides are known to bind with site I through hydrophobic interactions [55]. We transferred the Au@SGAN/SGD superlattice film onto a quartz disc and dried it at room temperature.…”

Section: (B)mentioning

confidence: 99%

Fluorescent superlattices of gold nanoparticles: A new class of functional materials

et al. 2009

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Fluorescent three-dimensional (3-D) superlattices of dansyl glutathione protected gold nanoparticles, with potential applications in molecular detection, have been synthesized at an air/water interface by controlling the pH of the nanoparticle suspension. The number of fl uorophores per nanoparticle was calculated to be ~127. Morphologies of the superlattice crystals were examined using scanning electron microscopy (SEM). Most of the crystals observed were triangular in shape. High-resolution transmission electron microscopy (HRTEM) and small angle X-ray scattering (SAXS) were used to study the packing of nanoparticles in these crystals. Both these studies showed that the nanoparticles were arranged in a face-centered cubic (fcc) pattern with a particle-particle distance (center-center) of ~10.5 nm. Evolution of the crystal morphologies with time was also examined. The fl uorescence properties of these triangles were studied using confocal fl uorescence imaging and confocal Raman mapping, which were in good agreement with the morphologies observed by SEM. The superlattice exhibits near-infrared (NIR) absorption in the range 1100-2500 nm. Easy synthesis of such functional nanoparticle-based solids makes it possible to use them in novel applications. We utilized the fl uorescence of dansyl glutathione gold superlattice crystals for the selective detection of bovine serum albumin (BSA), the major protein constituent of blood plasma, based on the selective binding of the naphthalene ring of the dansyl moiety with site I of BSA.

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“…The donor to acceptor distance in both environments is less than 7 nm, indicating a static quenching interaction between the donor and acceptor according to Förster's nonradiative energy transfer theory. 48 To understand and confirm the site-selective binding of DASPMI with BSA, known site selective binding ligands, dansylamide (DNSA) for site I (subdomain IIA) and dansylproline (DP) for site II (subdomain IIIA) 50 were used. Initial addition of DNSA in the BSA-DASPMI complex showed a gradual decrease in fluorescence intensity and reached saturation at 0.7 mM (Figure 10a).…”

Section: Resultsmentioning

confidence: 99%

Reverse Micelle Induced Flipping of Binding Site and Efficiency of Albumin Protein with an Ionic Styryl Dye

2010

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The effect of reverse micelle environment on the binding mechanism of 2-(4-(dimethylamino)styryl)-1-methylpyridinium iodide (DASPMI) with Bovine Serum Albumin (BSA) compared with that in buffer solution has been investigated in this paper with the help of steady state and time-resolved emission spectroscopy along with molecular docking to have a correct picture about binding. The binding of DASPMI with attachment efficiency of 30% and 70% at site I (subdomain IIA) and site II (subdomain IIIA) of BSA, respectively, in buffer solution gets reversed inside a reverse micelle. The bigger cavity size of site II in buffer solution ushers the dye with increased attachment efficiency and in reverse micelle change in π-stacking and hydrophobic interaction control the attachment efficiency. The calculated Förster distance gets curtailed as the environment changes from buffer to reverse micelle. The binding becomes stronger with a smaller gap between the probe and Trp-214 inside the reverse micelle than that in buffer solution.

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Synthesis, Photophysical Properties, in Vivo Photosensitizing Efficacy, and Human Serum Albumin Binding Properties of Some Novel Bacteriochlorins

Cited by 93 publications

References 32 publications

Fluorescence study on site-specific binding of perfluoroalkyl acids to human serum albumin

Fluorescence study on site-specific binding of perfluoroalkyl acids to human serum albumin

Fluorescent superlattices of gold nanoparticles: A new class of functional materials

Reverse Micelle Induced Flipping of Binding Site and Efficiency of Albumin Protein with an Ionic Styryl Dye

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