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Oxovanadium (IV) and diphenyltin (IV) complexes were synthesized on the nanoscale based on the Schiff base (H2L) derived from salicylaldehyde and d‐glucosamine. The complexes were formed with a molar ratio of 1:1 and 1:2 (metal: dligand) relative to oxovanadium (IV) and diphenyltin (IV), respectively. Fourier‐transform infrared spectroscopy, 1H and 13C nuclear magnetic resonance, mass fragmentations, electronic transitions, thermogravimetric analysis, and density functional theory were employed to validate the structure of synthesized compounds. The results demonstrated that the ligand (H2L) was successfully attached to oxovanadium (IV) and diphenyltin (IV) as di‐anionic and mono‐anionic ligands, respectively. The size of the complexes was investigated using the transmission scanning microscope. The work presents a prospective concept for the drug design of the targeted anticancer through the glucose moiety. All compounds revealed remarkable anticancer activities against the colorectal (HCT‐116) cell line, recording IC50 values 4.94, 21.73, and 62.5 μg/ml for VO (II)(L), free H2L, and Sn (ph)2(HL)2, respectively. The IC50 value of VO (II)(L) complex was increased after the quercetin inhibitor. Therefore, the sugar‐conjugated compound can be recognized by the glucose recognition binding site of GLUT and their cell‐killing effect depends highly on the GLUT inhibitor, quercetin. The potential GLUT transportability of the compounds was investigated through a molecular docking study. The anti‐migration activity was investigated for VO (II)(L) complex. The free ligand observed the best antimicrobial results. The antibacterial stimulation was investigated and represented different interaction types with the selected ribosyl transferase enzyme. [ABSTRACT FROM AUTHOR]

Nano‐structure Cu(II) complex [Cu(AMAB)2]Cl2 with Schiff base (AMAB) derived from the condensation between 4‐(dimethylamino)benzaldehyde and amoxicillin trihydrate was prepared. (AMAB) Schiff base and its Cu(II) complex were identified and confirmed by different physicochemical techniques. The Schiff base (AMAB) was coordinated to copper ion through carbonyl oxygen and imine nitrogen donor sites. X‐ray powder diffraction shows a cubic crystal system of the Cu(II) complex. The density functional theory was used to optimize the structure geometries of the investigated compounds. The molecular docking of the active amino acids of the investigated proteins' interactions with the tested compounds was evaluated. The bactericidal or bacteriostatic effect of the compounds was screened against some bacterial strains. The activity of Cu‐chelate against Gram‐negative bacteria was mainly more effective than its (AMAB) ligand and vice versa in the case of Gram‐positive bacteria. The biological activity of the prepared compounds with biomolecules calf thymus DNA (CT‐DNA) was determined by electronic absorption spectra and DNA gel electrophoresis technique. All studies revealed that the Cu‐chelate derivative exhibited better binding affinity to both CT‐DNA than the AMAB and amoxicillin itself. The anti‐inflammatory effect of the designed compounds was determined by testing their protein denaturation inhibitory activity spectrophotometrically. All obtained data supported that the designed nano‐Cu(II) complex with Schiff base (AMAB) is a potent bactericide against H. pylori, and exhibits anti‐inflammatory activity. The dual inhibition effects of the designed compound represent a modern therapeutic approach with extended spectrum of action. Therefore, it can act as good drug target in antimicrobial and anti‐inflammtory therapies. Finally, H. pylori resistance to amoxicillin is absent or rare in many countries, thus amoxicillin nanoparticles may be beneficial for countries where amoxicillin resistance is reported. [ABSTRACT FROM AUTHOR]

Autophagy functions in both selective and non‐selective ways to maintain cellular homeostasis. Endoplasmic reticulum autophagy (ER‐phagy) is a subclass of autophagy responsible for the degradation of the endoplasmic reticulum through selective encapsulation into autophagosomes. ER‐phagy occurs both under physiological conditions and in response to stress cues, and plays a crucial role in maintaining the homeostatic control of the organelle. Although specific receptors that target parts of the ER membrane, as well as, internal proteins for lysosomal degradation have been identified, the molecular regulation of ER‐phagy has been elusive. Recent work has uncovered novel regulators of ER‐phagy that involve post‐translational modifications of ER‐resident proteins and functional cross‐talk with other cellular processes. Herein, we discuss how morphology affects the function of the peripheral ER, and how ER‐phagy modulates the turnover of this organelle. We also address how ER‐phagy is regulated at the molecular level, considering implications relevant to human diseases. [ABSTRACT FROM AUTHOR]