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There are many benefits to drug delivery from drug–carrier nanostructure systems. It might be developed to carefully control drug release rates or to deliver a precise amount of a therapeutic substance to particular body areas. Self-assembling is the process by which molecules and nanoparticles spontaneously organize into organized clusters. For instance, proteins and peptides can interact with one another to create highly organized supramolecular structures with various properties, such as helical ribbons and fibrous scaffolds. Another advantage of self-assembly is that it may be effective with a variety of materials, including metals, oxides, inorganic salts, polymers, semiconductors, and even organic semiconductors. Fullerene, graphene, and carbon nanotubes (CNTs), three of the most fundamental classes of three-dimensionally self-assembling nanostructured carbon-based materials, are essential for the development of modern nanotechnologies. Self-assembled nanomaterials are used in a variety of fields, including nanotechnology, imaging, and biosensors. This review study begins with a summary of various major 3D nanomaterials, including graphene oxide, CNTs, and nanodiamond, as well as 3D self-assembled polyfunctionalized nanostructures and adaptable nanocarriers for drug delivery. [ABSTRACT FROM AUTHOR]

The current article is focused on introduction and validation of electro‐membrane extraction along with a high‐performance liquid chromatography combined with UV detector for the identification of the antiepileptic drugs phenytoin (PT) and phenobarbital (PB) in plasma, saliva, and urine. In addition, 3D‐printing was utilized to fabricate the designed caps required for fixing the electrodes in the prepared setup, giving us a high potential in device fabrication with various dimensions. To arrive at the highest extraction of PB and PT, the parameters impacting the extraction efficiency of electromembrane extraction for example, supported liquid membrane composition, sample solution pH, applied voltage, extraction time along with effect of graphene oxide are examined in detail. In optimized experimental conditions, the calibration plots were obtained to be linear on the concentration range of 25–500 ng/L with the detection limit and quantitation limit of 7.5 and 25 ng/L for both of PB and PT. Relative standard deviations of <9.9% and <9.1% were found for PB and PT, respectively and the enrichment factor for the presented method was computed to be 25.4 and 44.7 for PB and PT, respectively. The proposed method was satisfactorily employed in determination of PB and PT in plasma, urine and saliva. [ABSTRACT FROM AUTHOR]

Free radical polymerization is often used to prepare protein and peptide-loaded hydrogels for the design of controlled release systems and molecular imprinting materials. Peroxodisulfates (ammonium peroxodisulfates (APS) or potassium peroxodisulfates (KPS)) with N,N,N,N-tetramethylethylenediamine (TEMED) are frequently used as initiator and catalyst. However, exposure to these free radical polymerization reagents may lead to modification of the protein and peptide. In this work, we show the modification of lysine residues by ammonium peroxodisulfate (APS)/TEMED of the immunostimulant thymopentin (TP5). Parallel studies on a decapeptide and a library of 15 dipeptides were performed to reveal the mechanism of modification. LC-MS of APS/TEMED-exposed TP5 revealed a major reaction product with an increased mass (+12 Da) with respect to TP5. LC-MS(2) and LC-MS(3) were performed to obtain structural information on the modified peptide and localize the actual modification site. Interpretation of the obtained data demonstrates the formation of a methylene bridge between the lysine and arginine residue in the presence of TEMED, while replacing TEMED with a sodium bisulfite catalyst did not show this modification. Studies with the other peptides showed that the TEMED radical can induce methyleneation on peptides when lysine is next to arginine, proline, cysteine, aspargine, glutamine, histidine, tyrosine, tryptophan, and aspartic acid residues. Stability of peptides and protein needs to be considered when using APS/TEMED in in situ polymerization systems. The use of an alternative catalyst such as sodium bisulfite may preserve the chemical integrity of peptides during in situ polymerization.