Interaction between gliadins and anthocyan derivatives

Mazzaracchio, Palmira; Tozzi, Silvia; Boga, Carla; Forlani, Luciano; Pifferi, Pier Giorgio; Barbiroli, Giancarlo

doi:10.1016/j.foodchem.2011.05.084

Cited by 29 publications

(22 citation statements)

References 27 publications

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“…A suggested that the treatment with malvin induced a conformational rearrangement that involved a slight increase in α‐helix (from 39% to 41%), a significant increase in β‐sheet (from 13% to 27%) and a parallel decrease of the content of β‐turns (from 32% to 26%) and unordered structures (from 17% to 6%). These results are in agreement with the previously reported IR findings on analogous samples . The changes in the Amide III spectral range confirmed these trends: the component at 1254 cm −1 , assigned to unordered conformations, appeared less prominent upon the treatment (Fig.…”

Section: Resultssupporting

confidence: 93%

“…According to previous studies, the anthocyanin quantity absorbed by gliadins and the time for its complete absorption depend on the nature of the anthocyanin. The chosen conditions (i.e.…”

Section: Methodsmentioning

confidence: 94%

“…Gliadins were extracted from gluten with 70% ethanol/H 2 O (v/v) (modified Booth and Ewarth method), as reported elsewhere . The obtained gliadins are a mixture of α−, β−, γ − and ω − types…”

Section: Methodsmentioning

confidence: 99%

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Raman characterization of the interactions between gliadins and anthocyanins

Taddei

Zanna

Tozzi

2013

J Raman Spectroscopy

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Gliadins, the major proteins of the wheat flour, are a family of monomeric and disulphide‐bonded proteins formed by a non‐repetitive domain rich in α‐helix structures and heterogeneous repetitive domains rich in β‐reverse turns. Gliadins may be strong food allergens, and many studies have explored the mechanisms of gluten allergenicity, with the final aim to properly modify gluten proteins in order to decrease allergen immunoreactivity. In the present study, Raman spectroscopy was used to gain more insights into the conformational changes of gliadins upon interaction with different anthocyanins (kuromanin, callistephin, oenin, cyanin, pelargonin, malvin). Anthocyanins are powerful antioxidant molecules with anti‐carcinogenic properties and largely widespread natural colorants present in vegetables and flowers. Raman spectroscopy demonstrated that the anthocyanins under study induce in gliadins conformational changes of different extents. The treatment with malvin, kuromanin and callistephin induced significant changes in the tyrosine environment, while pelargonin, oenin and cyanin did not. The treatment with any of the anthocyanins altered the distribution of the disulphide conformations: the gauche‐gauche‐trans conformation increased at the expenses of the gauche‐gauche‐gauche conformation. Malvin and pelargonin provoked a significant decrease of the β‐turns content. Since both the latter structural elements have been related to gluten allergenicity, anthocyanins appeared interesting molecules, in the context of the attempts to modify gliadins with the aim to decrease allergen immunoreactivity. Copyright © 2013 John Wiley & Sons, Ltd.

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Section: Resultssupporting

confidence: 93%

“…According to previous studies, the anthocyanin quantity absorbed by gliadins and the time for its complete absorption depend on the nature of the anthocyanin. The chosen conditions (i.e.…”

Section: Methodsmentioning

confidence: 94%

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Raman characterization of the interactions between gliadins and anthocyanins

Taddei

Zanna

Tozzi

2013

J Raman Spectroscopy

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“…Electrospray ionization MS revealed the formation of soluble aggregates involving 2–6 anthocyanin units and 1–4 peptides (proline-rich proteins or histatin). STD-NMR was also used to investigate the binding of keracyanin (cyanidin 3-rutinoside) to wheat flour gliadins at pH = 2.5 [ 47 ]. Protons C2′-H, C5′-H, C6-H and C8-H appear to be primarily involved in the binding.…”

Section: The Basis Of Anthocyanin Chemistrymentioning

confidence: 99%

The Chemical Reactivity of Anthocyanins and Its Consequences in Food Science and Nutrition

2018

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Owing to their specific pyrylium nucleus (C-ring), anthocyanins express a much richer chemical reactivity than the other flavonoid classes. For instance, anthocyanins are weak diacids, hard and soft electrophiles, nucleophiles, prone to developing π-stacking interactions, and bind hard metal ions. They also display the usual chemical properties of polyphenols, such as electron donation and affinity for proteins. In this review, these properties are revisited through a variety of examples and discussed in relation to their consequences in food and in nutrition with an emphasis on the transformations occurring upon storage or thermal treatment and on the catabolism of anthocyanins in humans, which is of critical importance for interpreting their effects on health.

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“…[21] Moreover, the repetitive domains of gliadins consist of short repeated sequences, with high content of proline and glutamine, which are often considered as strong allergens. It has been reported that anthocyanins-gliadins complexes are very soluble in acidic conditions, [22] thus promoting the utilization of these proteins. However, researches concerning the binding of anthocyanins to gliadins, and the functional properties of their complexes are seldom reported.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of gliadins-diglycosylated cyanidins interaction from litchi pericarp through ultraviolet and fluorescence measurements

Zhu

Pinto

et al. 2017

International Journal of Food Properties

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The low stability of anthocyanins limits their use in industry, which can be surpassed by gliadins linkage. This work was aimed to study the anthocyanins-gliadins bonding properties. HPLC-DAD-ESI-MS 2 analysis indicated that the main litchi pericarp anthocyanin (LPA) was cyanidin-3-glucoside-5-rhamnoside (C3G5R). Ultraviolet and fluorescence data revealed the presence of anthocyanin-protein complexes, with strong binding affinity by a combination of hydrogen bonds and van der Waals forces. The combination of C3G5R and gliadins changed its secondary structure. The scavenging effect of the anthocyanin-protein complex over 2,2-diphenyl-1-picrylhydrazyl was comparable to LPA alone. These results may broaden gluten usage to stabilize anthocyanins and so their use in the food, pharmaceutic, and cosmetic industries due to their potential use as colorants and antioxidants.

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Interaction between gliadins and anthocyan derivatives

Cited by 29 publications

References 27 publications

Raman characterization of the interactions between gliadins and anthocyanins

Raman characterization of the interactions between gliadins and anthocyanins

The Chemical Reactivity of Anthocyanins and Its Consequences in Food Science and Nutrition

Evaluation of gliadins-diglycosylated cyanidins interaction from litchi pericarp through ultraviolet and fluorescence measurements

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