Polyethylene Glycol Functionalized Graphene Oxide Nanoparticles Loaded with Nigella sativa Extract: A Smart Antibacterial Therapeutic Drug Delivery System

Flaky graphene oxide (GO) nanoparticles (NPs) were synthesized using Hummer’s method and then capped with polyethylene glycol (PEG) by an esterification reaction, then loaded with Nigella sativa (N. sativa) seed extract. Aiming to investigate their potential use as a smart drug delivery system against Staphylococcus aureus and Escherichia coli, the spectral and structural characteristics of GO-PEG NPs were comprehensively analyzed by XRD, AFM, TEM, FTIR, and UV- Vis. XRD patterns revealed that GO-PEG had different crystalline structures and defects, as well as a higher interlayer spacing. AFM results showed GONPs with the main grain size of 24.41 nm, while GONPs–PEG revealed graphene oxide aggregation with the main grain size of 287.04 nm after loading N. sativa seed extract, which was verified by TEM examination. A strong OH bond appeared in FTIR spectra. Furthermore, UV- Vis absorbance peaks at (275, 284, 324, and 327) nm seemed to be correlated with GONPs, GO–PEG, N. sativa seed extract, and GO –PEG- N. sativa extract. The drug delivery system was observed to destroy the bacteria by permeating the bacterial nucleic acid and cytoplasmic membrane, resulting in the loss of cell wall integrity, nucleic acid damage, and increased cell-wall permeability.     

Effect of 1-Aminoanthracene (1-AMA) Binding on the Structure of Three Lipocalin Proteins,the Dimeric β Lactoglobulin,the Dimeric Odorant Binding Protein and the Monomeric α<Subscript>1</Subscript>-Acid Glycoprotein. Fluorescence Spectra and Lifetimes Studies

We studied effect of 1-aminoanthracene (1-AMA) binding on the structures of dimeric β lactoglobulin, dimeric odorant binding protein (OBP) and monomeric α₁-acid glycoprotein (lipocalin family proteins) by monitoring fluorescence excitation spectra and measuring fluorescence lifetimes of the tryptophan residues of the proteins. Results show that binding of 1-AMA to β lactoglobulin and OBP modifies their conformation even at low probe concentration compared to that of the proteins. Structural modification induces a red shift of the fluorescence excitation spectra maximum of tryptophan residues accompanied with an increase of the third fluorescence lifetime and a decrease of its pre-exponential factor. These effects were not observed for α₁-acid glycoprotein, probably as the result of carbohydrate presence. These data raise doubts concerning use of 1-AMA as a probe to study biological properties of β lactoglobulin and OBP.     

Origin of Fluorescence Lifetimes in Human Serum Albumin. Studies on Native and Denatured Protein

Human serum albumin consists of a single polypeptide of 585 amino acid residues with 1 Trp residue. In the present work, we measured fluorescence lifetimes of the protein in both native and denatured states. The results indicate that Trp emission occurs with three lifetimes in both states. Lifetimes values and contribution to the global emission decay differ between the two states. Data are interpreted as the results of an emission occurring from three substructures of the tryptophan formed in the excited state. Two of these substructures are already present for the tryptophan free in solution. The third lifetime is the result of the interaction between the tryptophan residue and surrounding microenvironment. The populations of these substructures characterized by the pre-exponential parameters of the fluorescence lifetimes are dependent on the fluorophore microenvironment and on the global protein structure.     

Fluorescence Lifetimes of Tryptophan: Structural Origin and Relation with So → 1Lb and So → 1La Transitions

We measured fluorescence lifetimes of L-Tryptophan dissolved in de-ionized water and in ethanol in the absence and the presence of high progesterone concentrations. The hormone absorbs between 220 and 280 with a peak around 250 nm, while its absorption is equal to zero beyond 280 nm. Tryptophan excitation spectrum recorded in presence of progesterone shows that the S_o → ¹L_a transition is completely abolished while the S_o → ¹L_b transition is not affected. Emission of L-tryptophan in water occurs with two fluorescence lifetimes, 0.40 and 2.8 ns. In ethanol, three fluorescence lifetimes equal to around 0.2, 1.8 and 4.8 ns were observed. Addition of progesterone to the medium does not affect any of the fluorescence lifetimes indicating clearly that both transitions could induce tryptophan excitation and that recorded fluorescence lifetimes could be assigned to sub-structures generated in the excited state.     

Electrochemical behavior and antioxidant activity of tetradentate Schiff bases and their copper(II) complexes

This study describes the effects of the substituents on electrochemical behavior and antioxidant activity of the six tetradentate Schiff bases, containing ethane-1,2-diamine or propane-1,2-diamine as the amine part and pentane-2,4-dione and/or 1-phenylbutane-1,3-dione as ??-diketone, and corresponding copper(II) complexes. Cyclic voltammograms of these compounds were recorded in dimethylsulfoxide and 0.1?M sodium perchlorate as supporting electrolyte with glassy carbon as working electrode at different scan rates. The voltammograms of Schiff bases alone showed only one irreversible peak. Voltammograms recorded for complexes showed the presence of quasi-reversible processes taking place at the metal center and reversible process at the ligand part. Both steric and inductive effects of substituents and structure of imine bridge of Schiff base ligands as well as complexes were discussed. These effects appear relevant for the antioxidant activity. Antioxidant activity of the investigated compounds expressed as Trolox equivalent antioxidant capacity is also discussed. The electrochemical behavior showed a high correlation with the antioxidant activity for investigated compounds.     

First synthesis and structural determination of a monomeric, unsolvated lithium amide, LiNH(2)

Alkali metal amides typically aggregate in solution and the solid phase, and even in the gas phase. In addition, even in the few known monomeric structures, the coordination number of the alkali metal is raised by binding of Lewis-basic solvent molecules, with concomitant changes in structure. In contrast, the simplest lithium amide LiNH(2) has never been made in a monomeric form, even though its structure has been theoretically predicted several times. Here, the first experimental structural data for a monomeric, unsolvated lithium amide are determined using a combination of gas-phase synthesis and millimeter/submillimeter-wave spectroscopy. All data point to a planar structure for LiNH(2). The r(o) structure of LiNH(2) has a Li-N distance of 1.736(3) A, an N-H distance of 1.022(3) A, and a H-N-H angle of 106.9(1) degrees. These results are compared with theoretical predictions for LiNH(2), and experimental data for oligomeric, solid-phase samples, which could not resolve the question of whether LiNH(2) is planar or not. In addition, comparisons are made with revised gas-phase and solid-phase data and calculated structures of NaNH(2).