Characterization of chitosan/Persian gum nanoparticles for encapsulation of Nigella sativa extract as an antiviral agent against avian coronavirus.

The aim of this study was to investigate the physicochemical characteristics of nanoparticles formed by the ionic gelation method between chitosan and water-soluble fraction of Persian gum (WPG) for encapsulation of Nigella sativa extract (NSE) as an antiviral agent. Our findings revealed that the particle size, polydispersity index (PDI), and zeta potential of the particles were in the range of 316.7-476.6 nm, 0.259-0.466, and 37.0-58.1 mV, respectively. The amounts of chitosan and WPG as the wall material and the NSE as the core had a considerable impact on the nanoparticle properties. The proper samples were detected at 1:1 chitosan:WPG mixing ratio (MR) and NSE concentration of 6.25 mg/mL. Fourier-transformed infrared (FTIR) spectroscopy proved the interactions between the two biopolymers. The effect of NSE on infectious bronchitis virus (IBV) known as avian coronavirus, was performed by the in-ovo method determining remarkable antiviral activity of NSE (25 mg/mL) and its enhancement through encapsulation in the nanoparticles. These nanoparticles containing NSE could have a promising capability for application in both poultry industry and human medicine as an antiviral product.

Design, synthesis, spectroscopic characterizations, antidiabetic, in silico and kinetic evaluation of novel curcumin-fused aldohexoses.

Curcumin (bis-α,ß-unsaturated ß-diketone) plays an important role in the prevention of numerous diseases, including diabetes. Curcumin, as an enzyme inhibitor, has ideal structural properties including hydrophobic nature, flexible backbone, and several available hydrogen bond (H-bond) donors and acceptors. In this study, curcumin-fused aldohexose derivatives 3(a-c) were synthesized and used as influential agents in the treatment of diabetes with inhibitory properties against two carbohydrate-hydrolyzing enzymes α-glucosidase (α-Gls) and α-amylase (α-Amy) which are known to be significant therapeutic targets for the reduction of postprandial hyperglycemia. These compounds were isolated, purified, and then spectrally characterized via FT-IR, Mass, 1H, and 13C NMR, which strongly confirmed the targeted product's formation. Also, their inhibitory properties against α-Gls and α-Amy were evaluated spectroscopically. The Results indicated that all compounds strongly inhibited α-Amy and α-Gls by mixed and competitive mechanisms, respectively. The intrinsic fluorescence of α-Amy was quenched by the interaction with compounds 1 and 3b through a dynamic quenching mechanism, and the 1 and 3b/α-Amy complexes were spontaneously formed, mainly driven by the hydrophobic interaction and hydrogen bonding. Fourier transform infrared spectra (FT-IR) comprehensively verified that the binding of compounds 1 and 3b to α-Amy would change the conformation and microenvironment of α-Amy, thereby inhibiting the enzyme activity. Docking and molecular dynamics (MD) simulations showed that all compounds interacted with amino acid residues located in the active pocket site of the proteins. In vivo studies confirmed the plasma glucose diminution after the administration of compound 3b to Wistar rats. Accordingly, the results of the current work may prompt the scientific communities to investigate the possibility of compound 3b application in the clinic.

LRH-1 (liver receptor homolog-1) derived affinity peptide ligand to inhibit interactions between ß-catenin and LRH-1 in pancreatic cancer cells: from computational design to experimental validation.

Poor prognosis, rapid progression and the lack of an effective treatment make pancreatic cancer one of the most lethal malignancies. Recent studies point to a role for liver receptor homolog-1 (LRH-1) in pathogenesis of pancreatic cancer and suggest prevention of the ß-catenin/LRH-1 complex formation as a potential strategy for inhibition of the pancreas cancer cells progression. In the current investigation, we have followed a biomimetic strategy and designed an affinity peptide with sequence DEMEEPQQTE to inhibit formation of the ß-catenin/LRH-1 complex. Quantitative real-time PCR experiments on the AsPC-1 pancreatic metastatic cells showed that the peptide has an inhibitory effect on the Wnt signaling proliferation line by reducing the expression levels of the CCND1, CCNE1, and MYC genes. Furthermore, the increased expression level of BAX gene showed that AsPC-1 cells were directed to the apoptosis pathway. At last, POU5F1, KLF4, and CD44 gene expression levels suggested that the peptide has an inhibitory effect on the stemness feature of the AsPC-1 cells. Here, we introduced a novel peptide inhibitor targeting an important protein-protein interaction, the ß-catenin/LRH-1 complex, which may provide highly promising starting points for subsequent drug design. Communicated by Ramaswamy H. Sarma.

Synthesis and spectroscopic characterization of new sulfanilamide-functionalized magnetic nanoparticles, and the usability for carbonic anhydrase purification: is there perspective for 'cancer treatment' application?

This investigation indicated an efficient procedure to purify human carbonic anhydrase II (hCA II) enzyme through sulfanilamide-functionalized (γ-Fe2O3-CPTES-SA) magnetic nanoparticles (MNPs), where synthesis of Fe3O4 MNPs was carried out using co-precipitation reaction. Next, 3-chloropropyltriethoxysilane (CPTES) was used to modify Fe3O4 nanoparticles and lastly, the surface of the nanoparticles was functionalized with sulfanilamide (SA) as a carbonic anhydrase ligand/inhibitor for binding to hCA II. The characterization of the synthesized nanoparticles was performed using various techniques. These characterization methods revealed that the MNPs were effectively coated with CPTES and SA, and the average diameter of the nanoparticles was approximately 21 nm. The possibility of interaction of γ-Fe2O3-CPTES-SA nanoparticles with hCA II was studied via multi-spectroscopic techniques. The protein isolated by this single-step procedure had high purity as confirmed by a single band on SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) which was also active after purification. By focusing on their drug loading capacity, and increasing their specificity and affinity to target CA-expressing cancer cells, the synthesized MNPs may dramatically impact the treatment of cancer and become suitable for clinical use in the near future.Communicated by Ramaswamy H. Sarma.