Relaxation Editing in NMR Using a New Two-Dimensional Long-Lived Coherence Method for Mixture Analysis.

The exploration of metabolomics and targeted segments of proteins stands as a pivotal facet of Nuclear Magnetic Resonance (NMR) analysis, furnishing valuable insights into molecular architectures and potential therapeutic applications. The issue of spectral congestion frequently presents challenges in ascribing distinct peaks within the confines of both one-dimensional (1D) and two-dimensional (2D) NMR spectra. Numerous strategies have been proposed to resolve specific resonances in NMR spectra differentially. Among these approaches, relaxation editing emerges as a viable solution. In the realm of relaxation phenomena within NMR, Long-Lived States (LLS) and Long-Lived Coherences (LLC) manifest as promising phenomena, offering enhanced relaxation lifetimes in comparison to the traditional longitudinal (T1) and transverse (T2) relaxation times for coupled nuclear spins. Notably, LLC presents a pathway to attenuate uncoupled high-intensity peaks, effectively diminishing their impact. The foundation of this technique rests upon the premise that the relaxation lifetime in the rotating frame (T1ρ) remains smaller than TLLC. In pursuit of refining spectral assignments within complex mixtures, we introduce a new pulse sequence tailored for LLC Total Correlation Spectroscopy (LLC-TOCSY). This demonstrates efficacy in extracting LLC signals within configurations involving multiple coupled spins, thereby decluttering the spectrum and enhancing the accuracy of peak assignments. To validate the effectiveness of this method, a collection of samples was subjected to scrutiny, yielding compelling results.

Phase controlled green synthesis of wurtzite (P63mc) ZnO nanoparticles: interplay of green ligands with precursor anions, anisotropy and photocatalysis.

Green approaches for nanosynthesis often lack the precise control of synthetic outcomes, which is primarily due to the poorly defined reaction protocols. Herein, we investigated the use of lignocellulosic agro-waste, sugarcane press mud (PM), for the synthesis of ZnO nanoparticles using three different precursor salts and their further application in the photocatalytic degradation of rhodamine dyes. This approach resulted in the formation of ZnO nanoparticles with two different morphologies, i.e., sheet-like structure from the zinc sulphate and nitrate precursors, whereas sphere-like structures from zinc acetate. In all three cases, the wurtzite phase (P63mc) of ZnO nanoparticles remained consistent. Also, the ZnO nanoparticles were found to be positively charged ("ζ" = +8.81 to +9.22 mv) and nearly monodispersed, with a size and band gap in the range of ∼14-20 nm and 3.78-4.1 eV, respectively. Further, the potential photocatalytic activity of these nanoparticles was investigated under direct sunlight. At the same photocatalyst dose of 0.1 g L-1, the three ZnO nanoparticles showed varying efficiencies due to their shape anisotropy. The ZnO NPs from acetate salt (∼20 nm, sheet like) showed the highest dye degradation efficiency (90.03%) in 4.0 hours, indicating the role of the catalyst-dye interface in designing efficient photocatalysts.

Bispidine as a promising scaffold for designing molecular machines.

The development of artificial molecular machines is a challenging endeavor. Herein, we have synthesized a series of bispidine diamides D1-D6 that exhibit rotation reminiscent of a motor motion. Dynamic NMR, X-ray diffraction, quantum mechanical calculations, and molecular dynamics simulations provided insights into their rotational dynamics. All the diamides D1-D6 exhibited mutually independent rotation around the two bispidine arms. However, the rate of rotation and the presence or absence of directionality in amide bond rotation were found to depend on the solvent, temperature, and nature of substitution on the amide carbonyl. These engineered systems may aid in the development of biologically relevant synthetic molecular motors. Studies on homochiral and heterochiral bispidine-peptides revealed that the direction of rotation can be controlled by chirality and the nature of the amino acid.

Long-Lived States Provide Insights from NMR into the ß-Cyclodextrin Drug Assemblies.

In the last two decades, extending spin memory in NMR has been used for several purposes. Long-lived states (LLS) or singlet states are one of the first spin memory enhancement techniques used. LLS have the potential to extract structural information and intra- and intermolecular interactions of complex systems other than studying slow phenomenon. The motional regime of ß-cyclodextrin (ß-CD) drug inclusion complexes generally lies in the intermediate region, where ωτc ≈ 1, and the standard methods of studying these interactions, i.e., NOE and chemical shift monitoring, suffer from insufficient output information. The sensitivity of LLS toward the environmental changes is utilized here to gain insights into the drug assemblies formed by ß-CD. One can use change in relaxation of LLS to study the structural changes during complexation. The examples of ß-CD with the drugs indomethacin, paracetamol, gliclazide, and CI-933 (a precursor 4-methoxybenzamide) were studied. Indomethacin, paracetamol, and 4-methoxybenzamide show strong interaction through the para-substituted benzene ring, unlike gliclazide. Relaxation of LLS in ß-CD-drug complexes is modeled using standard Redfield Relaxation Theory. Computational studies performed support the experimental observations. Docking and molecular dynamics simulation provided the explanation of the relaxation properties of these drug molecules.

Bispidine as a ß-strand nucleator: from a ß-arch to self-assembled cages and vesicles.

The development of synthetic scaffolds that nucleate well-folded secondary structures is highly challenging. Herein, we designed and synthesized a series of core-modified peptides (F1, F2, F3, and F4) that fold into ß-strand structures. These bispidine-scaffolded peptides were studied by CD, IR, NMR, single crystal XRD, and Molecular Dynamics (MD) simulations to investigate their conformational preferences. Solid-state and solution studies revealed that bispidine is a versatile scaffold that could be placed either at the terminal or at the middle of the peptide strand for nucleating the ß-strand structure. Scaffolds that nucleate an isolated ß-strand conformation are rare. Bispidine placed at the C-terminus of the peptide chain could nucleate a ß-strand conformation, while bispidine placed at the middle resulted in a ß-arch conformation. This nucleation activity stems from the ability to restrict the psi torsion angle (ψ) through intramolecular C5 hydrogen bonding between the equatorial hydrogen(s) of bispidine and the carbonyl oxygen(s) of the amino acid close to the scaffold. Furthermore, the bispidine peptidomimetic with a super secondary structure, namely ß-arch, assembled into single-hole submicron cages and spherical vesicles as evident from microscopic studies. The design logic defined here will be a significant strategy for the development of ß-strand mimetics and super secondary structures.