Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers

Dandurand, Jany; Samouillan, Valérie; Lacoste-Ferré, Marie-Hélène; Lacabanne, C.; Bochicchio, Brigida; Pepe, Antonietta

doi:10.1016/j.patbio.2014.02.001

Cited by 52 publications

(41 citation statements)

References 50 publications

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“…570 °C. These results are in agreement with results published by Rocha et al, 14 pertaining to thermogravimetric analysis of crude sericin extracts from plain Bombyx mori cocoons, and Dandurand et al, 28 pertaining to the thermogravimetric analysis of peptide fragments. The 1 st derivative of the weight loss curve (i.e., the rate of mass change, Figure 2b) can be used to tell the points at which weight loss is most apparent (inflection points) ( Table 5).…”

Section: Thermal Analyses Via Tga and Dscsupporting

confidence: 93%

“…Mass decrements during heating were evaluated from thermogravimetric curves, whereas the temperature of the maximum rate of mass change (T max ) was determined from the maximum of the 1 st derivative of the weight loss curves. According to Dandurand et al, 28 the global trend of the thermogravimetric plot depicted in purple in Figure 2a (viz., lyophilized sericin) corresponds to the classical thermal behavior of a freeze-dried protein. The first stage, occurring between 25 and 100 °C (Figure 2a), is generally linked to the evaporation of water adsorbed to the protein moieties, and corresponds to ca.…”

Section: Thermal Analyses Via Tga and Dscmentioning

confidence: 96%

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Structural and Functional Stabilization of Sericin from Bombyx mori Cocoons in a Biopolysaccharide Film: Bioorigami for Skin Regeneration

Balcão

Harada

Jorge

et al. 2020

J. Braz. Chem. Soc.

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Development and optimization of a bioorigami film with silk sericin was pursued for skin regeneration. Several formulations were produced, with varying integrated sericin contents, viz. 0, 1, 2, 5, 10, 20 and 50 mg sericin mL film-1. The physico-chemical characteristics of the bioorigami films produced were evaluated via infrared spectrophotometry, X-ray diffraction, X-ray transmission, X-ray fluorescence, thermogravimetry, differential scanning calorimetry, transdermal protein permeation, kinetics of protein release from the bioorigami films and free radical scavenging activities. The mechanical resistance was also evaluated. The results by 2,2-diphenyl-1-picrylhydrazil (DPPH) assay suggest that the bioorigami films integrating crude sericin extract had capacity to sequester free radicals, exhibited prolonged release of the bioactive protein, good physico-chemical characteristics and adequate mechanical resistance. Specifically, the bioorigami film with 10 mg sericin mL film-1 proved to be able to release all the bioactive protein in a 12 h timeframe. The results suggest potential for use in biopharmaceutical application, specifically, as material for use in hydrogels.

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Section: Thermal Analyses Via Tga and Dscsupporting

confidence: 93%

Section: Thermal Analyses Via Tga and Dscmentioning

confidence: 96%

Structural and Functional Stabilization of Sericin from Bombyx mori Cocoons in a Biopolysaccharide Film: Bioorigami for Skin Regeneration

Balcão

Harada

Jorge

et al. 2020

J. Braz. Chem. Soc.

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“…The first was observed immediately after the temperature increase, ending at~100 • C and associated with water elimination from the sample [18]. The second weight loss, which occurred between 200 and 300 • C, was due to sample degradation (except for the glycerol, which started at 150 • C), namely, progressive deamination, decarboxylation, and depolymerization arising from the breaking of polypeptide bonds [21]. This range is to be expected for myofibrillar proteins according to Rocha et al [22].…”

Section: Thermogravimetric Analysis (Tga)mentioning

confidence: 99%

Effect of Different Polyalcohols as Plasticizers on the Functional Properties of Squid Protein Film (Dosidicus Gigas)

et al. 2019

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Conventional plastic materials accumulation has led to a constant search to develop friendly packaging, edible coatings from biopolymers are an example. Since different proteins have different behavior and plastizicer compatibility, in this work, the effect of different polyalcohols (glycerol, sorbitol, maltitol, mannitol, and xylitol) as plasticizers on squid protein films behavior was studied. The results show that except for mannitol, transparent, and flexible films can be obtained. None of them showed transmission to light on the ultraviolet (UV) spectrum. However, only glycerol and sorbitol were sufficiently flexible to evaluate their mechanical properties, in which glycerol had a more elastic behavior with an elongation at a break of 920% and tensile strength (TS) of 0.94 MPa, while sorbitol exhibited a more plastic behavior with an elongation at break of 511% and a TS of 4.41 MPa. Water-vapor transmission rate was higher in glycerol, with 194.41 g·m−2d−1, while sorbitol had 44.27 g·m−2d−1 but presented blooming. This could be due to low interaction between sorbitol and the protein matrix, correlating with the film-solubility results. Amide I band of the Fourier transform infrared (FT-IR) spectra demonstrated higher denaturation and loss of alpha helical structure in glycerol film, followed by maltitol/sorbitol, xylitol, mannitol, and the control film. This in accordance with thermogravimetric analysis (TGA) results. The results of this study prove that only glycerol and sorbitol are suitable to obtain a see-through flexible film.

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“…[17,18] Finally, the very low protein amounts in the suspensions where the fibrils appeared (0.1 mg/L and 10 μg/L samples contain 6-8 μg/L and 0.6-0.8 μg/L of protein(s), respectively) is some orders of magnitude lower than that incurred using, for example, circular dichroism, infrared spectroscopy, calorimetry and dye-binding characterization techniques. [19][20][21][22] Although the fibrils formation rate is proportional to the amount of biopolymer, [23] fibrils were predominant only at very low concentrations of our purified samples (Figures 2, 4, and 5). To explain this apparent paradox we propose a mechanism of pigment self-assembly dependent on protein(s)-eumelanin interactions ( Figure 6).…”

Section: Resultsmentioning

confidence: 81%

Effect of Melanomal Proteins on Sepia Melanin Assembly

Srisuk

Correlo

Leonor

et al. 2015

Journal of Macromolecular Science, Part B

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Keywords Downloaded by [Dalhousie University] at 08:36 11 October 2015 ACCEPTED MANUSCRIPT ACCEPTED MANUSCRIPT 2 Sepia melanin self-assembly; amyloid fibrils; cephalopod ink; scanning electron microscopy; Scanning transmission electron microscopy; Atomic force microscopy. ABSTRACT Melanins are phenol-based pigments with the potential for widespread applications including bioelectronics and tissue engineering. The concentration-dependent structural transition of sepia melanin in water is analyzed. This biopolymer at high concentration gives the well-known nanospheres, whereas sample dilution gives unforeseen nanofibres exhibiting the structural features of mature amyloid fibrils. We propose a mechanism of pigment self-assembly dependent on the interaction of residual melanosomal protein(s) with eumelanin heteropolymer. Our results contribute to understanding the peculiar physico-chemical properties of this ubiquitous pigment. Downloaded by [Dalhousie University] at 08:

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Conformational and thermal characterization of a synthetic peptidic fragment inspired from human tropoelastin: Signature of the amyloid fibers

Abstract: FT-IR and thermal techniques are well suited to evidence conformational and structural differences between the soluble peptide and its amyloid form.

Cited by 52 publications

References 50 publications

Structural and Functional Stabilization of Sericin from Bombyx mori Cocoons in a Biopolysaccharide Film: Bioorigami for Skin Regeneration

Structural and Functional Stabilization of Sericin from Bombyx mori Cocoons in a Biopolysaccharide Film: Bioorigami for Skin Regeneration

Effect of Different Polyalcohols as Plasticizers on the Functional Properties of Squid Protein Film (Dosidicus Gigas)

Effect of Melanomal Proteins on Sepia Melanin Assembly

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