The utility of Hibiscus sabdariffa L. to prepare metal oxides NPs for clinical application on osteoporosis supported by theoretical study.

Green synthesis of metal oxides as a treatment for bone diseases is still exploring. Herein, MgO and FeO NPs were prepared from the extract of Hibiscus sabdariffa L. to study their effect on vit D, Ca, and alkaline phosphatase enzyme ALP associated with osteoporosis.

Experimental and density functional theory studies on some metal oxides and the derived nanoclusters: a comparative effects on human ferritin.

A comprehensive investigation into the green synthesis of metal oxide nanoparticles (NPs) has garnered significant attention due to its commendable reliability, sustainability, and environmentally friendly attributes. Green synthesis methods play a crucial role in mitigating the adverse effects associated with conventional approaches employed for nanostructure preparation. This research endeavors to examine the impact of ginger plant extract-assisted green synthesis of metal oxides NPs on the serum ferritin levels of anemic diabetic patients in vitro, focusing specifically on α-FeO and ZnO NPs.

Antiureolytic activity of new water-soluble thiadiazole derivatives: Spectroscopic, DFT, and molecular docking studies.

Two new water-soluble thiadiazole compounds are prepared and characterized with various techniques. These compounds, 5-amino-1,3,4-thiadiazole hydrochloride (1) and 5-amino-3-(N-propane-2-imine)-1,3,4-thiadiazole chloride salt (2) were synthesized via Mannich reaction, and characterized by microelemental analysis, and some spectroscopic means (FTIR, UV-Vis, H NMR, C NMR and mass), in addition to single-crystal X-ray diffraction for compound 2. DFT calculations were conducted to study their geometry optimization, vibrational spectra, MEP maps, and NBO analysis.

Transition of Nano-Architectures Through Self-Assembly of Lipidated β-Tripeptide Foldamers.

β-peptides consisting exclusively of β-amino acids adopt a variety of non-natural helical structures and can self-assemble into well-defined hierarchical structures by axial head-to-tail self-assembly resulting in fibrous materials of varying sizes and shapes. To allow control of fiber morphology, a lipid moiety was introduced within a tri-β-peptide sequence at each of the three amino acid positions and the N-terminus to gain finer control over the lateral assembly of fibers. Depending on the position of the lipid, the self-assembled structures formed either twisted ribbon-like fibers or distinctive multilaminar nanobelts.

The CDR1 and Other Regions of Immunoglobulin Light Chains are Hot Spots for Amyloid Aggregation.

Immunoglobulin light chain-derived (AL) amyloidosis is a debilitating disease without known cure. Almost nothing is known about the structural factors driving the amyloidogenesis of the light chains. This study aimed to identify the fibrillogenic hotspots of the model protein 6aJL2 and in pursuing this goal, two complementary approaches were applied.

Evaluation of Some Trace Elements and Vitamins in Major Depressive Disorder Patients: a Case-Control Study.

Major depressive disorder (MDD) is a common mental disorder worldwide; however, little is known about its etiology. It is well known that levels of certain trace elements are associated with the pathogenesis of some diseases. Accordingly, this study aims to evaluate the effect of trace elements and vitamins in the etiology of MDD.

Identifying the Coiled-Coil Triple Helix Structure of β-Peptide Nanofibers at Atomic Resolution.

Peptide self-assembly represents a powerful bottom-up approach to the fabrication of nanomaterials. β-Peptides are non-natural peptides composed entirely of β-amino acids, which have an extra methylene in the backbone, and we reported fibers derived from the self-assembly of β-peptides that adopt 14-helical structures. β-Peptide assemblies represent a class of stable nanomaterials that can be used to generate bio- and magneto-responsive materials with proteolytic stability.

The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.

Amyloidogenic peptides are well known for their involvement in diseases such as type 2 diabetes and Alzheimer's disease. However, more recently, amyloid fibrils have been shown to provide scaffolding and protection as functional materials in a range of organisms from bacteria to humans. These roles highlight the incredible tensile strength of the cross-β amyloid architecture.

Chemically and thermally stable silica nanowires with a β-sheet peptide core for bionanotechnology.

Background: A series of amyloidogenic peptides based on the sequence KFFEAAAKKFFE template the silica precursor, tetraethyl orthosilicate to form silica-nanowires containing a cross-β peptide core.

Results: Investigation of the stability of these fibres reveals that the silica layers protect the silica-nanowires allowing them to maintain their shape and physical and chemical properties after incubation with organic solvents such as 2-propanol, ethanol, and acetonitrile, as well as in a strong acidic solution at pH 1.5.

Silica Nanowires Templated by Amyloid-like Fibrils.

Many peptides self-assemble to form amyloid fibrils. We previously explored the sequence propensity to form amyloid using variants of a designed peptide with sequence KFFEAAAKKFFE. These variant peptides form highly stable amyloid fibrils with varied lateral assembly and are ideal to template further assembly of non-proteinaceous material.

Silica Nanowires Templated by Amyloid-like Fibrils.

Many peptides self-assemble to form amyloid fibrils. We previously explored the sequence propensity to form amyloid using variants of a designed peptide with sequence KFFEAAAKKFFE. These variant peptides form highly stable amyloid fibrils with varied lateral assembly and are ideal to template further assembly of non-proteinaceous material.