Corn zein undergoes conformational changes to higher β-sheet content during its self-assembly in an increasingly hydrophilic solvent

Erickson, Daniel P.; Ozturk, Oguz Kaan; Selling, Gordon W.; Feng, C. Q.; Campanella, Osvaldo H.; Hamaker, Bruce R.

doi:10.1016/j.ijbiomac.2020.04.169

Cited by 34 publications

(23 citation statements)

References 43 publications

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“…This is in line with the FTIR secondary structure analysis showing an increase in β-sheet content with increasing proportion of zein in the dough samples ( Table 1 ). Similar results have been obtained by Erickson et al (2020a) , who reported an increase in ThT fluorescence intensity at increasing β-sheet secondary structure percentages in zein-ethanol solutions. An et al (2016) also observed an increase in ThT fluorescence intensity by fibrillation of α-zein upon thermal incubation.…”

Section: Resultssupporting

confidence: 90%

“… Erickson et al, 2020a , Erickson et al, 2020b recently showed that the presence of non-fibril dense β-sheet structures could also lead to the observed increase in ThT emission intensity. However, the fluorescence emission of dough samples excited at 280 nm ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In addition, due to its relatively large surface area available for an ordered hydrogen bond formation, β-sheet structures may play an important part in the formation of protein fibrillar aggregates and have been reported to be the signature structural feature of protein fibrils ( Erickson et al, 2012 ; Krebs et al, 2005 ; Pinotsi et al, 2016 ). It has been suggested that zein proteins tend to form insoluble β-sheet rich fibrils in a dough system which are responsible for the viscoelasticity of zein polymers ( Chen et al, 2021 ; Erickson et al, 2012 , 2020a ; King et al, 2016 ; Taylor et al, 2013 ). The formation of fibrils by zein proteins in the here studied dough systems was supported by ThT fluorescence experiments.…”

Section: Discussionmentioning

confidence: 99%

“…The results point to the presence of a higher structured fibrillar network with zein addition to the dough samples, providing more binding sites for ThT ( Biancalana and Koide, 2010 ). The ThT fluorescence intensity has been reported to be positively correlated with the percentage of β-sheet secondary structure ( Erickson et al, 2020a ). The β-sheet structures in protein fibrils are likely interconnected and stabilized by a dense network of hydrogen bonds ( Fig.…”

Section: Discussionmentioning

confidence: 99%

See 3 more Smart Citations

Vibrational and fluorescence spectroscopy to study gluten and zein interactions in complex dough systems

Sadat

Corradini

Joye

2022

Current Research in Food Science

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Vibrational and fluorescence spectroscopy to study gluten and zein interactions in complex dough systems

Sadat

Corradini

Joye

2022

Current Research in Food Science

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“…During EISA, the size of zein microspheres was observed to increase because of the hydrophobic interactions between the zein molecules owing to the contribution of hydrophilicity and hydrophobicity to the interfacial free energy. Moreover, Erickson et al 33 also studied the structural changes occurring during the self-assembly process, and it was found that the increased hydrophilicity of the solvent-induced self-assembly of zein into spherical aggregates with a diameter of 0.1−1.0 μm. In addition, the α-helix decreased in favor of β-sheets during the process.…”

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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Investigation of the binding interactions mechanism between zein with chrysin by multispectroscopic techniques

Gao

Cheng

et al. 2023

J of Molecular Recognition

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As a natural carrier protein, zein was intensively studied for the construction of a flavonoid delivery system. Chrysin has presented superior tumor‐resistant, anti‐inflammatory, and anti‐oxidation potentials among the flavonoid candidates in clinical practice. However, due to inadequate research, the binding mechanism and structural affinity of zein to chrysin are still indeterminate. Therefore, multispectral methods were employed to explore the molecular interaction of zein and chrysin in this work. These techniques showed that chrysin reduced the intrinsic fluorescence of zein via a static process and that the interaction between zein and chrysin was mainly driven spontaneously by hydrophobic forces. Additionally, the experimental results revealed the changed microenvironment in the vicinity of tyrosine and affected secondary structure in the presence of chrysin, indicating zein's conformation were altered by chrysin. This work provided comprehensive insight into the combination of plant‐derived protein (zein) and flavonoids (chrysin) and helped rationalize the protection, transportation, and release of chrysin through a zein‐based delivery system.

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Corn zein undergoes conformational changes to higher β-sheet content during its self-assembly in an increasingly hydrophilic solvent

Cited by 34 publications

References 43 publications

Vibrational and fluorescence spectroscopy to study gluten and zein interactions in complex dough systems

Vibrational and fluorescence spectroscopy to study gluten and zein interactions in complex dough systems

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

Investigation of the binding interactions mechanism between zein with chrysin by multispectroscopic techniques

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