Solution conformational analysis of the alpha-zein proteins of maize.

Tatham, Arthur S.; J, Field; Morris, Victor J.; I'Anson, K.J.; Cardle, Linda; Dufton, Mark J.; Shewry, Peter R.

doi:10.1016/s0021-9258(19)74308-7

Cited by 94 publications

(81 citation statements)

References 26 publications

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“…Zein, a major storage protein of corn, has emerged as a promising biomaterial because of its low cost, abundance, amphipathy, biodegradability, biocompatibility, and nontoxicity. , Based on different structures and properties, zein can be classified into four types as α-zein, β-zein, γ-zein, and δ-zein. Among these, α-zein is the most abundant component reaching 75–85% with molecular weights of 19 kDa (Z19) and 22 kDa (Z22) as well as a trace amount of dimer (39 kDa). − α-zein exhibits unique solubility because of the high proportion (>50%) of nonpolar amino acids (e.g., Leucine, alanine, proline, and phenylalanine). , It demonstrates insolubility in most solvents except binary mixtures of alcohol and water with appropriate compositions (60–95 vol % of alcohol), − aqueous methanol, isopropanol, propylene glycol, and acetone. − Among these, ethanol is the most commonly used solvent because of safety and easy recovery.…”

Section: Introductionmentioning

confidence: 99%

Study on Self-Assembled Morphology and Structure Regulation of α-Zein in Ethanol–Water Mixtures

et al. 2020

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α-Zein has received widespread attention owing to its unique solubility, amphipathic, and self-assembly properties, which is because of its high proportion of nonpolar amino acids and unique amino acid sequence. The protein self-assembly is a significant and widely observed phenomenon in many scientific areas such as food and biomedicine, among many industries. In this study, we investigated the self-assembly behavior of α-zein and regulated the morphology and structure of the self-assembled α-zein by varying the experimental parameters like pH, ethanol content, induction time, and α-zein concentration during the self-assembly process in ethanol–water mixtures. The nanospheres and nanofibers were observed under different conditions [nanospheres observed under acidic and strongly alkaline (pH > 10.5) conditions or for ethanol content lower than 65% and higher than 75%; nanofibers observed under weakly alkaline (pH 9.5–10.5) conditions or for 65–75% ethanol concentration for induction duration longer than 24 h]. The morphological and structural analyses of the self-assembled α-zein showed that the self-assembly process was accompanied by the transformation of the morphology and conformation of α-zein. The studies on the self-assembly process and mechanism revealed that α-zein first self-assembled into nanospheres, followed by the nanospheres adhering to shape-beaded fibers and finally fibers, accompanied by a structural transformation from the disordered into ordered state. The nanosphere formation is noted to follow the nucleation-based polymerization, and the nanosphere-mediated mechanisms lead to the formation of nanofibers. Moreover, the hydrophobic interactions, hydrogen bonds, and electrostatic interactions are concluded to drive the α-zein self-assembly. The findings from this study are expected to provide a theoretical basis for expanding the commercial applications of α-zein.

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Section: Introductionmentioning

confidence: 99%

Study on Self-Assembled Morphology and Structure Regulation of α-Zein in Ethanol–Water Mixtures

et al. 2020

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“…[16][17][18][19][20] Zein, a predominant storage protein of corn, is capable of self-assembly and is insoluble in water but readily dispersed in alcohol-water mixtures due to its unusual amino acid sequence which contains highly hydrophobic residues. [21][22][23][24] Zein is a potential candidate biomaterial scaffold for bone regeneration with various interesting properties, such as biocompatibility, degradability, and excellent mechanical properties (toughness, flexibility, and compressibility), antioxidant activity and resistance to microbial attack. [18][19][20][25][26][27][28][29] Based on its properties, zein has also been used in various biomedical applications, such as edible packaging materials, carriers for drug delivery, and adhesives.…”

Section: Introductionmentioning

confidence: 99%

Biomimetic mineralization of zein/calcium phosphate nanocomposite nanofibrous mats for bone tissue scaffolds

Zhang

Mao

et al. 2014

CrystEngComm

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“…The irradiation of proteins can involve both inter- and intra-crosslinking, resulting from a variety of reactions, including carbon–carbon crosslinking of the backbone, aromatic crosslinking, and even the formation of new disulfide bridges between cystines [ 21 , 22 , 23 , 24 ]. For Zein in particular, aromatic crosslinking (such as by tyrosine formation) is anticipated to be the predominant mechanism if crosslinking is present due to the oxygen-rich environment in which these studies were conducted, as well as the negligible amounts of sulfur-containing amino acids found in Zein [ 21 , 25 , 26 ]. In order to further evaluate the presence of crosslinking, SDS-PAGE was performed.…”

Section: Resultsmentioning

confidence: 99%

Gold–Protein Composite Nanoparticles for Enhanced X-ray Interactions: A Potential Formulation for Triggered Release

et al. 2021

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Drug-delivery vehicles have been used extensively to modulate the biodistribution of drugs for the purpose of maximizing their therapeutic effects while minimizing systemic toxicity. The release characteristics of the vehicle must be balanced with its encapsulation properties to achieve optimal delivery of the drug. An alternative approach is to design a delivery vehicle that preferentially releases its contents under specific endogenous (e.g., tissue pH) or exogenous (e.g., applied temperature) stimuli. In the present manuscript, we report on a novel delivery system with potential for triggered release using external beam radiation. Our group evaluated Zein protein as the basis for the delivery vehicle and used radiation as the exogenous stimulus. Proteins are known to react with free radicals, produced during irradiation in aqueous suspensions, leading to aggregation, fragmentation, amino acid modification, and proteolytic susceptibility. Additionally, we incorporated gold particles into the Zein protein matrix to create hybrid Zein–gold nanoparticles (ZAuNPs). Zein-only nanoparticles (ZNPs) and ZAuNPs were subsequently exposed to kVp radiation (single dose ranging from 2 to 80 Gy; fractionated doses of 2 Gy delivered 10 times) and characterized before and after irradiation. Our data indicated that the presence of gold particles within Zein particles was correlated with significantly higher levels of alterations to the protein, and was associated with higher rates of release of the encapsulated drug compound, Irinotecan. The aggregate results demonstrated a proof-of-principle that radiation can be used with gold nanoparticles to modulate the release rates of protein-based drug-delivery vehicles, such as ZNPs.

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Solution conformational analysis of the alpha-zein proteins of maize.

Cited by 94 publications

References 26 publications

Study on Self-Assembled Morphology and Structure Regulation of α-Zein in Ethanol–Water Mixtures

Study on Self-Assembled Morphology and Structure Regulation of α-Zein in Ethanol–Water Mixtures

Biomimetic mineralization of zein/calcium phosphate nanocomposite nanofibrous mats for bone tissue scaffolds

Gold–Protein Composite Nanoparticles for Enhanced X-ray Interactions: A Potential Formulation for Triggered Release

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