Spectral demonstration of structural transitions in albumins

Tankovskaia, Svetlana A.; Abrosimova, Karina V.; Пастон, С. В.

doi:10.1016/j.molstruc.2018.05.100

Cited by 7 publications

(4 citation statements)

References 33 publications

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“…The addition of nitric acid C = 0.63 M caused a strong change in the amide I band in the region 1620–1640 cm −1 (Figure 2) corresponding to β-sheets [53]. There were also less noticeable changes that could be studied in more detail by deconvolution of the second derivatives of the spectra (Figure 1b).…”

Section: Resultsmentioning

confidence: 99%

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Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

et al. 2019

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Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

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Section: Resultsmentioning

confidence: 99%

“…The temperature of 90 °C in combination with an alkaline solution (1M KOH) of HSA (20% w / w ) for 1 min caused a significant reduction of the α-helix [53] and an increment of β-sheets (Table 7). Unlike alkaline denaturation without heating, random coil content is expected [65].…”

Section: Resultsmentioning

confidence: 99%

Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

et al. 2019

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“…(5) Except for in the pure pig glue, there were marked enhancements in CH3 symmetric bending vibration peaks (1377~1403 cm −1 ), which were important signs of aging [38]. Large amounts of research have proven that light and thermal aging would result in the decrease of α-helix, the increase of β-sheet, and random coils [42][43][44][45]. This signifies that the ordered structure of proteins transforms into disordered states, partially because the bonds' vibrations are intensive, the stretching and bending energy are increasing, and the spatial structure becomes loose with the increase in temperature.…”

Section: Spectral Changesmentioning

confidence: 99%

The Influence of Natural Aging Exerting on the Stability of Some Proteinaceous Binding Media Commonly Used in Painted Artworks

Yang

Wang

et al. 2022

Coatings

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Natural aging plays a key role in the degradation of proteinaceous binders which are important dispersers and stabilizers of painting layers. Knowledge about the natural aging influence on the stability of binders is important for exploring the deterioration mechanisms of painted artworks. Pig glue, whole egg, egg white, egg yolk, casein, and mixtures with ultramarine were aged for 10 years in natural conditions. GC-MS and FTIR were applied to explore the changes in the binders at a molecular level. Our experiment revealed that the less stable Met (Methionine), Lys (Lysine), Ile (Isoleucine), Ser (Serine), Asp (Aspartic acid), Glu (Glutamic acid), Hyp (Hydroxyproline), especially aromatic Phe (Phenylalanine), and Tyr (Tyrosine) were damaged, thus the contents of the stable Ala (Alanine), Gly (Glycine), Val (Valine), Leu (Leucine), and Pro (Proline) increased. The broadening of Amide A and the declining amount of α-helix, along with the increasing contents of β-sheet and random coils, all showed that the binders had transformed into disordered states. What is more, we found that pig glue had better natural aging resistance, ultramarine could speed up the aging process and lipids in egg were more easily degraded. The mechanisms of the changes of primary structures and secondary structures are also discussed in the paper.

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“…One of the substances used as the basis for the production of foams is albumin [3]. It is the most important protein in the chicken egg and belongs to the family of globular single-chain proteins [4]. Food foams made on the basis of albumin show low mechanical strength [5] and thermodynamic instability [6].…”

Section: Wpływ Dodatku Gumy Ksantanowej I Gumy Guar Na Właściwości Rementioning

confidence: 99%

The impact of addition of xanthan gum and guar gum on rheological properties of foams produced by continuous method

Kabziński¹,

Neupauer

Nowak³

et al. 2019

Polimery

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The paper presents the effect of the addition of hydrocolloids-xanthan gum and guar gum-on the rheological properties of ovoalbumin-based food foams, produced by continuous method. The foaming was carried out in a column apparatus with additional aeration equipped with a paddle stirrer. In order to determine the rheological parameters, a hysteresis loop test was carried out. The results of the study were described using the Ostwald-de Waele equation. The effect of the addition of hydrocolloid on the rheological properties of the obtained foams was characterized, and the synergistic effects between the hydrocolloids used were described.

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Spectral demonstration of structural transitions in albumins

Cited by 7 publications

References 33 publications

Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

The Influence of Natural Aging Exerting on the Stability of Some Proteinaceous Binding Media Commonly Used in Painted Artworks

The impact of addition of xanthan gum and guar gum on rheological properties of foams produced by continuous method

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