Acetylcholinesterase is a prime target for therapeutic intervention in Alzheimer's disease. Acetylcholinesterase inhibitors (AChEIs) are used to improve cognitive abilities, playing therefore an important role in disease management. Drug repurposing screening has been performed on a corporate chemical library containing 11 353 compounds using a target fishing approach comprising three-dimensional (3D) shape similarity and pharmacophore modeling against an approved drug database, Drugbank. This initial screening identified 108 hits. Among them, eight molecules showed structural similarity to the known AChEI drug, pyridostigmine. Further structure-based screening using a pharmacophore-guided rescoring method identifies one more potential hit. Experimental evaluations of the identified hits sieve out a highly selective AChEI scaffold. Further lead optimization using a substructure search approach identifies 24 new potential hits. Three of the 24 compounds (compounds 10b, 10h, and 10i) based on a 6-(2-(pyrrolidin-1-yl)pyrimidin-4-yl)-thiazolo[3,2-a]pyrimidine scaffold showed highly promising AChE inhibition ability with IC50 values of 13.10 ± 0.53, 16.02 ± 0.46, and 6.22 ± 0.54 μM, respectively. Moreover, these compounds are highly selective toward AChE. Compound 10i shows AChE inhibitory activity similar to a known Food and Drug Administration (FDA)-approved drug, galantamine, but with even better selectivity. Interaction analysis reveals that hydrophobic and hydrogen-bonding interactions are the primary driving forces responsible for the observed high affinity of the compound with AChE.We present a comprehensive experimental study of a di-t-butyl-substituted cyclooctatetraene-based molecular balance to measure the effect of 16 different solvents on the equilibrium of folded versus unfolded isomers. In the folded 1,6-isomer, the two t-butyl groups are in close proximity (H···H distance ≈ 2.5 Å), but they are far apart in the unfolded 1,4-isomer (H···H distance ≈ 7 Å). We determined the relative strengths of these noncovalent intramolecular σ-σ interactions via temperature-dependent nuclear magnetic resonance measurements. The origins of the interactions were elucidated with energy decomposition analysis at the density functional and ab initio levels of theory, pinpointing the predominance of London dispersion interactions enthalpically favoring the folded state in any solvent measured.A unique 1D nanostructure of Pt@CeO2-BDC was prepared from Pt@CeBDC MOF. The Pt@CeO2-BDC was rich in oxygen vacancies (i.e., XPS Oβ/(Oα + Oβ) = 39.4%), and on the catalyst, the 2 nm Pt clusters were uniformly deposited on the 1D mesoporous polycrystalline CeO2. Toluene oxidation was conducted in a spectroscopic operando Raman-online FTIR reactor to elucidate the reaction mechanism and establish the structure-activity relationship. The reaction proceeds as follows (I) adsorption of toluene as benzoate intermediates on Pt@CeO2-BDC at low temperature by reaction with surface peroxide species; (II) reaction activation and ring-opening involving lattice oxygen with a concomitant change in defect densities indicative of surface rearrangement; (III) complete oxidation to CO2 and H2O by lattice oxygen and reoxidation of the reduced ceria with consumption of adsorbed oxygen species. The Pt clusters, which mainly exist as Pt2+ with minor amounts of Pt0 and Pt4+ on the surface, facilitated the adsorption and reaction activation. The Pt-CeO2 interface generates reduced ceria sites forming nearby adsorbed peroxide at low temperature that oxidize toluene into benzoate species by a Langmuir-Hinshelwood mechanism. As the reaction temperature increases, the role of lattice oxygen becomes important, producing CO2 and H2O mainly by the Mars-van Krevelen mechanism.The concept of metal chelation is based on simple coordination chemistry. The development of an ideal metal chelator that completely and selectively removes toxic metals from a specific metal binding site in proteins is required to prevent and or inhibit a variety of diseases, among them neurodegenerative diseases. This work examines neuropeptide Y (NPY) as a Zn2+ and Cu2+ chelator agent. NPY is a natural peptide that is produced in the human body; therefore, it is not a toxic agent and the complex that it forms is not toxic as well. Our simulations reveal that NPY has an efficient Zn2+ chelation activity but is less effective in chelating Cu2+. Moreover, while NPY demonstrates several conformations, the metal chelation occurs more efficiently in its native structure. Beyond the exploration of the activity of NPY as a Zn2+ and Cu2+ chelator agent, this work provides an insight into the molecular mechanisms of the chelation of these metals at the molecular level. The outcomes from this work may guide future experimental studies to examine NPY in metal chelation therapy for neurodegenerative diseases.The crystals of a novel family of rare-earth borate-nitrate compounds, Ln7(BO3)3(NO3)N3O (Ln = Pr, Nd), were grown at high-pressure in KAs flux and their crystal structure was determined. The new type of the crystalline structure consists of parallel chains of Ln6 octahedra connected by common faces and forming the channels with the NO3 triangular planar motifs in the center, and isolated OLn4 tetrahedra separated from each other by N3 triangular motifs. Each NO3 triangle is in fact a part of rather unusual (NB3O12) block consisting of 3 distorted BO4 tetrahedra around central nitrogen atom. Under near-infrared (NIR) ( λ ex = 1064 nm) excitation, both compounds revealed a strong signal of second harmonic generation (SHG) at half the excitation wavelength ( λ em = 532 nm), which is in agreement with their noncentrosymmetric structure. S3I-201 In addition, a photon up-conversion (UC) emission at λ em = 880 nm was observed for microcrystals of Nd7(BO3)3(NO3)N3O, which was assigned to the UC process occurring within the 4f electronic manifold of Nd3+ ions. The dual-emission (SHG/UC) properties of Nd7(BO3)3(NO3)N3O microcrystals, concomitant with the absence of photobleaching, makes them prospective candidates for microscopic probes in biological studies.