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A prolamin paralog generated upon maize whole-genome duplication has changed its polymerization and solubility properties, allowing a new function in the assembly of maize protein bodies. Abstract In the lumen of the endoplasmic reticulum (ER), prolamin storage proteins of cereal seeds form very large, ordered heteropolymers termed protein bodies (PBs), which are insoluble unless treated with alcohol or reducing agents. In maize PBs, 16-kD γ-zein locates at the interface between a core of alcohol-soluble α-zeins and the outermost layer mainly composed of the reduced-soluble 27-kD γ-zein. 16-kD γ-zein originates from 27-kD γ-zein upon whole-genome duplication and is mainly characterized by deletions in the N-terminal domain that eliminate most Pro-rich repeats and part of the Cys residues involved in inter-chain bonds. 27-kD γ-zein also forms insoluble PBs when expressed in transgenic vegetative tissues. We show that in Arabidopsis leaves, 16-kD γ-zein assembles into disulfide-linked polymers that fail to efficiently become insoluble. Instead of forming PBs, these polymers accumulate as very unusual threads that markedly enlarge the ER lumen, resembling amyloid-like fibers. Domain-swapping between the two γ-zeins indicates that the N-terminal region of 16-kD γ-zein has a dominant effect in preventing full insolubilization. Therefore, a newly evolved prolamin has lost the ability to form homotypic PBs, and has acquired a new function in the assembly of natural, heteropolymeric PBs.

This research investigated the potential of zein–sodium caseinate–diosmin nanoparticles (ZCD-NPs) as an anti-cancer agent against the A2780 cell line. Dynamic light scattering (DLS) analysis showed that ZCD-NPs have an average size of 265.30 nm with a polydispersity index of 0.21, indicating good uniformity suitable for pharmaceutical applications. Fourier transform infrared spectroscopy (FTIR) confirmed the successful incorporation of diosmin into the NPs and highlighted the interactions between the components. Field emission scanning electron microscopy (FESEM) images showed spherical NPs with smooth surfaces, suggesting stability and high production quality. Encapsulation efficiency was remarkably high, at 93.45%. Cytotoxicity assays showed a dose-dependent effect of ZCD-NPs, with A2780 cells showing significant sensitivity compared to normal HDF cells, indicating selective targeting of cancer cells. Flow cytometry analysis confirmed that ZCD-NPs induced apoptosis and necrosis in A2780 cells, as evidenced by increased expression of apoptotic genes such as p53 and caspases 8 and 9. In addition, ZCD-NPs exhibited potent antioxidant activity, effectively scavenging free radicals. These results suggest that ZCD-NPs have promising properties for targeted cancer therapy and antioxidant applications, which warrant further exploration in clinical settings.

Zein, a corn‐derived prolamine protein, has become a powerful ally in the fight against cancer, particularly non‐small cell lung cancer (NSCLC.) Its unique attributes, enriched by modifiable hydroxyl and amino groups, have led to the development of advanced functionalised drug delivery systems. Innovative techniques like chemical crosslinking, desolvation, dispersion and micromixing have led to the creation of zein‐based nanoparticles, revolutionising cancer therapy. Central to this examination is the remarkable ability of zein NPs to enhance drug stability, optimise oral bioavailability and improve targeted drug delivery, specifically tailored to combat NSCLC. This represents not just a technological breakthrough but a paradigm shift, ushering in a new era of precise, personalised and effective cancer treatment. Zein, a hydrophobic nanoparticle, is a promising drug for cancer treatment. However, its journey to the clinic is challenging due to its hydrophobic nature and the need for advanced evaluative platforms. This review emphasises the need for rigorous research to align zein's potential with real‐world applications. It offers a synthesis of methodologies, applications, and obstacles, aiming to see zein nanoparticles as a central element in cancer therapy innovations. The review encourages researchers, clinicians and industry professionals to embrace the potential of zein and promote the convergence of laboratory innovation and clinical application.

Essential amino acids like lysine and tryptophan are deficient in corn meal because of the abundance of zein storage proteins that lack these amino acids. A natural mutant, opaque 2 (o2) causes reduction of zeins, an increase of nonzein proteins, and as a consequence, a doubling of lysine levels. However, o2's soft inferior kernels precluded its commercial use. Breeders subsequently overcame kernel softness, selecting several quantitative loci (QTLs), called o2 modifiers, without losing the high-lysine trait. These maize lines are known as \"quality protein maize\" (QPM). One of the QTLs is linked to the 27-kDa γ-zein locus on chromosome 7S. Moreover, QPM lines have 2- to 3-fold higher levels of the 27-kDa γ-zein, but the physiological significance of this increase is not known. Because the 27- and 16-kDa γ-zein genes are highly conserved in DNA sequence, we introduced a dominant RNAi transgene into a QPM line (CM105Mo2) to eliminate expression of them both. Elimination of γ-zeins disrupts endosperm modification by o2 modifiers, indicating their hypostatic action to γ-zeins. Abnormalities in protein body structure and their interaction with starch granules in the F1 with Mo2/+; o2/o2; γRNAi/+ genotype suggests that γ-zeins are essential for restoring protein body density and starch grain interaction in QPM. To eliminate pleiotropic effects caused by o2, the 22-kDa α-zein, γ-zein, and β-zein RNAis were stacked, resulting in protein bodies forming as honeycomb-like structures. We are unique in presenting clear demonstration that γ-zeins play a mechanistic role in QPM, providing a previously unexplored rationale for molecular breeding.

Lecithin, a naturally small molecular surfactant, which is widely used in the food industry, can delay aging, enhance memory, prevent and treat diabetes. The interaction between zein and soy lecithin with different mass ratios (20:1, 10:1, 5:1, 3:1, 2:1, 1:1 and 1:2) in ethanol-water solution and characterisation of zein and lecithin composite colloidal nanoparticles prepared by antisolvent co-precipitation method were investigated. The mean size of zein-lecithin composite colloidal nanoparticles was firstly increased with the rise of lecithin concentration and then siginificantly decreased. The nanoparticles at the zein to lecithin mass ratio of 5:1 had the largest particle size (263 nm), indicating that zein and lecithin formed composite colloidal nanoparticles, which might aggregate due to the enhanced interaction at a higher proportion of lecithin. Continuing to increase lecithin concentration, the zein-lecithin nanoparticles possibly formed a reverse micelle-like or a vesicle-like structure with zein in the core, which prevented the formation of nanoparticle aggregates and decreased the size of composite nanoparticles. The presence of lecithin significantly reduced the ζ-potential of zein-lecithin composite colloidal nanoparticles. The interaction between zein and lecithin enhanced the intensity of the fluorescence emission of zein in ethanol-water solution. The secondary structure of zein was also changed by the addition of lecithin. Differential scanning calorimetry thermograms revealed that the thermal stability of zein-lecithin nanoparticles was enhanced with the rise of lecithin level. The composite nanoparticles were relatively stable to elevated ionic strengths. Possible interaction mechanism between zein and lecithin was proposed. These findings would help further understand the theory of the interaction between the alcohol soluble protein and the natural small molecular surfactant. The composite colloidal nanoparticles formed in this study can broaden the application of zein and be suitable for incorporating water-insoluble bioactive components in functional food and beverage products.

Maize (Zea mays) zeins are some of the most abundant cereal seed storage proteins (SSPs). Their abundance influences kernel hardness but compromises its nutritional quality. Transcription factors regulating the expression of zein and other SSP genes in cereals are endosperm-specific and homologs of maize opaque2 (O2) and prolamine-box binding factor (PBF). This study demonstrates that the ubiquitously expressed transcription factors, O2 heterodimerizing proteins (OHPs), specifically regulate 27-kD γ-zein gene expression (through binding to an O2-like box in its promoter) and interact with PBF. The zein content of double mutants OhpRNAi;o2 and PbfRNAi;o2 and the triple mutant PbfRNAi;OhpRNAi;o2 is reduced by 83, 89, and 90%, respectively, compared with the wild type. The triple mutant developed the smallest zein protein bodies, which were merely one-tenth the wild type’s size. Total protein levels in these mutants were maintained in a relatively constant range through proteome rebalancing. These data show that OHPs, O2, and PBF are master regulators of zein storage protein synthesis, acting in an additive and synergistic mode. The differential expression patterns of OHP and O2 genes may cause the slight differences in the timing of 27-kD γ-zein and 22-kD α-zein accumulation during protein body formation.

EGCG is a catechin known for its antioxidant and anti-inflammatory characteristics. Vitamin B12 is an essential vitamin found in animal-derived products, and its deficiency may cause serious health problems such as anemia. The effectiveness of both catechin and vitamin B12 depends on their stability and bioavailability, which can be lost during industrial processes due to degradation when exposed to external factors. A potential solution to this issue is the microencapsulation, which protects the compounds from external agents. The current study aims to microencapsulate EGCG and vitamin B12 in a polymer matrix of biological origin, zein. Microencapsulation was performed using an electrospinning technique, and different concentrations of zein (1–30% w/v) and active compound (0.5–5% w/w) were tested, resulting in the production of micro/nanoparticles, fibers, or the mixture of both. The microstructures were analyzed and characterized in terms of morphology, release profile and kinetics, and encapsulation efficiency. High encapsulation efficiencies were obtained, and the highest were found in the samples with 1% w/w of active substance and 30% w/v of zein. Controlled release studies were conducted in deionized water and in an ethanolic solution, and five kinetic models were applied to the release profiles. The results indicated that the Weibull model was the best fit for the majority of results.

Summary Maize kernels do not contain enough of the essential sulphur‐amino acid methionine (Met) to serve as a complete diet for animals, even though maize has the genetic capacity to store Met in kernels. Prior studies indicated that the availability of the sulphur (S)‐amino acids may limit their incorporation into seed storage proteins. Serine acetyltransferase (SAT) is a key control point for S‐assimilation leading to Cys and Met biosynthesis, and SAT overexpression is known to enhance S‐assimilation without negative impact on plant growth. Therefore, we overexpressed Arabidopsis thaliana AtSAT1 in maize under control of the leaf bundle sheath cell‐specific rbcS1 promoter to determine the impact on seed storage protein expression. The transgenic events exhibited up to 12‐fold higher SAT activity without negative impact on growth. S‐assimilation was increased in the leaves of SAT overexpressing plants, followed by higher levels of storage protein mRNA and storage proteins, particularly the 10‐kDa δ‐zein, during endosperm development. This zein is known to impact the level of Met stored in kernels. The elite event with the highest expression of AtSAT1 showed 1.40‐fold increase in kernel Met. When fed to chickens, transgenic AtSAT1 kernels significantly increased growth rate compared with the parent maize line. The result demonstrates the efficacy of increasing maize nutritional value by SAT overexpression without apparent yield loss. Maternal overexpression of SAT in vegetative tissues was necessary for high‐Met zein accumulation. Moreover, SAT overcomes the shortage of S‐amino acids that limits the expression and accumulation of high‐Met zeins during kernel development.

Grain starch and protein are synthesized during endosperm development, prompting the question of what regulatory mechanism underlies the synchronization of the accumulation of secondary and primary gene products. We found that two endosperm-specific NAC transcription factors, ZmNAC128 and ZmNAC130, have such a regulatory function. Knockdown of expression of ZmNAC128 and ZmNAC130 with RNA interference (RNAi) caused a shrunken kernel phenotype with significant reduction of starch and protein. We could show that ZmNAC128 and ZmNAC130 regulate the transcription of Bt2 and then reduce its protein level, a rate-limiting step in starch synthesis of maize endosperm. Lack of ZmNAC128 and ZmNAC130 also reduced accumulation of zeins and nonzeins by 18% and 24% compared with nontransgenic siblings, respectively. Although ZmNAC128 and ZmNAC130 affected expression of zein genes in general, they specifically activated transcription of the 16-kDa γ-zein gene. The two transcription factors did not dimerize with each other but exemplified redundancy, whereas individual discovery of their function was not amenable to conventional genetics but illustrated the power of RNAi. Given that both the Bt2 and the 16-kDa γ-zein genes were activated by ZmNAC128 or ZmNAC130, we could identify a core binding site ACGCAA contained within their target promoter regions by combining Dual-Luciferase Reporter and Electrophoretic Mobility Shift assays. Consistent with these properties, transcriptomic profiling uncovered that lack of ZmNAC128 and ZmNAC130 had a pleiotropic effect on the utilization of carbohydrates and amino acids.

This study intends to conduct both in-vitro and in-silico investigations to assess the bioactivity of newly developed zein/sodium alginate (SA) composite beads. These beads, prepared using the dropwise method, were infused with different concentrations (10%, 20%, 30%, and 40%) of bioglass (BG). These BG-loaded zein/SA- composites were formed into beads with calcium chloride (CaCl 2 , 5%) as a crosslinking agent. The resulting composite beads were characterized using various techniques (XRD, FTIR, SEM, and EDXA) both before and after in vitro testing in Simulated Body Fluid (SBF). A 3D model of zein was constructed using I-TASSER and validated through PROCHECK and ERRAT servers. The interaction forces between the zein protein and sodium alginate were analyzed in silico using molecular docking with Autodock vina and PyMOL software. The results showed that the formation of a hydroxyapatite (HA) layer on the surface of the BG-loaded zein/SA composite beads confirmed their biological activity, which increased with higher BG content. The results suggest that zein/SA composite beads loaded with bioglass (BG), exhibiting good bioactivity, are suitable for use in bio-tissue engineering applications. A molecular docking study revealed that sodium alginate (SA) can interact with zein through van der Waals forces and hydrogen bonds, leading to the formation of stable complexes. This zein/SA complex is well-suited for carrying bioglass (BG) and has potential applications as a drug carrier in a drug delivery system. Based on the results, our study shows that BG-loaded Zein/SA composite beads are bioactive materials, and can be used in tissue engineering and improve the deposition of new HA, consequently enhancing bone generation. In addition, the prepared composite beads can serve as an excellent drug carrier (future work).