A Novel Rhodamine-Phenolphthalein Architecture for Selective Mercury Ion Detection in Aqueous Media.

In this study, the primary objective is to synthesize a novel fluorescent Rh-PP-Rh compound and explore its extensive range of photochemical behaviors. Initially, the synthesis of the novel Rh-PP-Rh was carried out for this purpose. Subsequently, UV-Vis and fluorescence spectroscopy were employed to investigate the interactions between Rh-PP-Rh and a diverse array of ions in aqueous solvent systems. Through fluorescence and UV-Vis studies, it was observed that Rh-PP-Rh demonstrated turn-on sensor properties in the presence of Hg2+ ions. Furthermore, the limits of detection (LOD) and association constant (Ka) values for Rh-PP-Rh/Hg2+ were determined as 334 nM and 9.13×1011 M-2, respectively. Additionally, the reversible studies demonstrated a switchable on/off response upon alternate addition of HgCl2 and [Bu4N]F to Rh-PP-Rh. These findings suggest that the probe Rh-PP-Rh also possesses specific sensor properties for F- ions in the presence of mercury. In addition, the investigation encompassed an assessment of the visual analysis of the color alterations of Rh-PP-Rh both on filter paper and in an EtOH/H2O solution. The findings demonstrated that Rh-PP-Rh can be successfully utilized in solutions containing mercury, as it generates significant color transformations.

The isolation of secondary metabolites from Rheum ribes L. and the synthesis of new semi-synthetic anthraquinones: Isolation, synthesis and biological activity.

Rheum ribes L. (Rhubarb) is one of the most important edible medicinal plants in the Eastern Anatolia region and is called "Iskin" by local people. Resveratrol and 6-O-methylalaternin were isolated from the Rhubarb for the first time in addition to well-known secondary metabolites including emodin, aloe-emodin, ß-sitosterol and rutin. The new semi-synthetic anthraquinone derivatives with the NαFmoc-l-Lys and ethynyl group were synthesized from the isolated anthraquinones emodin and aloe-emodin of Rhubarb to increase the bioactivities. Aloe-emodin derivative with NαFmoc-l-Lys shows the highest inhibition values by 94.11 ± 0.12 and 82.38 ± 0.00% against HT-29 and HeLa cell lines, respectively, at 25 µg/mL. Further, modification of the aloe-emodin with both the ethynyl and the NαFmoc-l-Lys groups showed an antioxidant activity-enhancing effect. From molecular docking studies, the relative binding energies of the emodin and aloe-emodin derivatives to human serum albumin ranged from -7.30 and -10.62 kcal/mol.

Biophysical study of phloretin with human serum albumin in liposomes using spectroscopic methods.

The ability of drugs to diffuse through the lipid bilayer of cell membranes is important for their metabolism, distribution, and efficacy. In this study, the interaction between phloretin and human serum albumin (HSA) in an L-egg lecithin phosphatidylcholine (PC) liposome suspension was investigated by fluorescence and absorbance spectroscopy. The spectroscopic and fluorescence quenching experiments show that phloretin molecules penetrated into the lumen of the liposome. The partition coefficient of phloretin in the PC liposome suspensions was calculated from fluorescence quenching measurements. The results show that phloretin efficiently quenches the intrinsic fluorescence of HSA through a combination of dynamic and static quenching. The values of Gibbs free energy, and the enthalpy and entropic change in the binding process of phloretin with HSA in the PC liposome suspensions were negative, suggesting that the binding process of phloretin and HSA was spontaneous. Hydrogen bonding and van der Waals force interactions play an important role in the interaction between the two molecules. In addition, binding of phloretin to HSA in liposome suspensions was investigated by synchronous fluorescence spectroscopy.

A novel pyrene-based selective colorimetric and ratiometric turn-on sensing for copper.

Detection of copper attracts important in most environmental and biological systems. In this study, a simple probe BisPyTSC containing bis-pyrene core was synthesized, and cation binding and sensing properties were studied using colorimetric and fluorometric detection. The research indicated that the specific ligand affinity for Cu2+ ions results in drastic color and spectral changes. According to the data obtained, while the peak intensity increases at 376 nm, the peak intensity decreased at 280 nm in the absorption spectrum of BisPyTSC and an increase in fluorescence intensity of BisPyTSC was observed in the presence of Cu2+ ions. The binding ratio of BisPyTSC to Cu2+ was found to be 1:1 according to Job's plot experiments. The binding constant was calculated using the Benesi-Hildebrand equation and found to be 3.26 × 104 M-1. Based on these concentration dependent fluorescence changes, the limit of detection (LOD) value was calculated to be 14.5 µM for Cu2+, which is the range of copper that should be in the blood (11.8-23.6 µM). As a result of all these studies, we can understand that BisPyTSC is a good selective candidate turn-on sensor that can be used for Cu2+ detection.

Spectroscopic investigations on the binding of Pyronin Y to human serum albumin.

The interaction of Pyronin Y with human serum albumin (HSA) has been investigated systematically by fluorescence, absorption, fluorescence decay lifetime measurements, FTIR, synchronous fluorescence spectroscopy, and molecular modeling method. The spectroscopic and fluorescence quenching experiments show that Pyronin Y may show a static quenching mechanism with HSA. The specific binding distance of 1.96 nm between HSA and Pyronin Y was obtained via Förster non-radiation energy transfer method. The thermodynamic parameters indicate that the electrostatic interactions play a significant role during the binding process. In addition, synchronous fluorescence and FT-IR spectra indicated that the conformation and microenvironment of HSA were not influenced with the addition of Pyronin Y. The obtained results can be of biological significance in photodynamic therapy.

Fluorescence study on the interaction of human serum albumin with Butein in liposomes.

The interaction of Butein with human serum albumin in L-egg lecithin phosphatidycholine (PC) liposome has been investigated by fluorescence and absorption spectroscopy. The results of the fluorescence measurement indicated that Butein effectively quenched the intrinsic fluorescence of HSA via static quenching. The Stern­Volmer plots in all the liposome solutions showed a positive deviation from the linearity. According to the thermodynamic parameters, the hydrophobic interactions appeared be the major interaction forces between Butein and HSA. The effect of Butein on the conformation of HSA was also investigated by the synchronous fluorescence under the same experimental conditions. In addition, the partition coefficient of the Butein in the PC liposomes was also determined by using the fluorescence quenching process. The obtained results can be of biological significance in pharmacology and clinical medicine.

The investigation of the interaction between orientin and bovine serum albumin by spectroscopic analysis.

In this paper, the interaction between orientin and bovine serum albumin (BSA) was examined using fluorescence and absorbance spectroscopy. The analysis of the quenching mechanism was done using Stern-Volmer plots which exhibit upward (positive) deviation. A linear response to orientin was shown in the concentration range between 3 and 50 µM. The experimental results showed the presence of a static quenching process between orientin and BSA. The thermodynamic parameters ΔH, ΔS and ΔG were also calculated and suggested that the hydrophobic and electrostatic interactions played an important role in the interaction between orientin and BSA. Furthermore, the distances between BSA and orientin were determined according to Förster non-radiation energy transfer theory. In addition, the results of the synchronous fluorescence obtained indicated that the binding of orientin with BSA could affect conformation in BSA.

Spectroscopic studies on the interaction of fluorescein and safranine T in PC liposomes.

In this study, the fluorescence quenching of fluorescein by safranine T in liposome media had been investigated systematically by fluorescence spectroscopy, UV-vis absorption spectroscopy and fluorescence decay lifetime measurements. The spectroscopic data were analyzed using a Stern-Volmer equation to determine the quenching process. The experimental results showed that the intrinsic fluorescence of fluorescein was strongly quenched by safranine T, and that the quenching mechanism was considered as static quenching by forming a ground-complex. The Stern-Volmer quenching constant Ksv, and the bimolecular quenching constant Kq were estimated. The distances between the donor (fluorescein) and the acceptor (safranine T) were calculated according to the Förster non-radiation energy transfer theory. In addition, the partition coefficient of the safranine T (Kp) in the L-egg lecithin phosphatidylcholine liposomes was also calculated by utilizing the fluorescence quenching.