Influence of pigments and protein aging on protein identification in historically representative casein-based paints using enzyme-linked immunosorbent assay

Ren, Fang; Atlasevich, Natalya; Baade, Brian; Loike, John D.; Arslanoglu, Julie

doi:10.1007/s00216-015-9089-0

Cited by 27 publications

(21 citation statements)

References 36 publications

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“…The complexity of matrices and the poor solubility of aged proteins challenge the separation of the protein fraction from the inorganic part [7]. Complexation with pigments, aggregation as well as cross-linking phenomena, further affects protein solubility, thus affecting the amount of retrievable protein [4,[29][30][31][32][33]. Moreover, casein is characterized by a high level of hydrophobicity, a relatively high charge, a limited α-helix and β-sheet secondary structure, and its solubility is strongly pH dependent (minimal solubility at pH 4.5 with a gradual increase with alkalinization) [34,35].…”

Section: Discussionmentioning

confidence: 99%

Sidestepping the challenge of casein quantification in ancient paintings by dot-blot immunoassay

Cattò

Gambino

Cappitelli

et al. 2017

Microchemical Journal

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A straightforward procedure based on dot-blot immunoassay is proposed as an effective diagnostic tool suitable for detecting and quantifying milk casein in cultural heritage samples. A polyclonal primary antibody, denaturing conditions and the standard addition method were used to overcome barriers common to the traditional analysis of protein-based artistic materials, providing the possibility of achieving specific and detailed results in an easy and cost effective way. The optimized procedure detected, and successfully quantified, casein in both freshly dried and artificially aged model samples prepared with milk casein and various pigments (azurite, calcite, cinnabar, minium and red ochre). Moreover, the experiments revealed that pigments as well as artificial ageing did not differently influence the dot-blot response. Thermogravimetric analysis confirmed the obtained results. The detection and quantification of casein applied to canvas 70-years ago for conservation purposes provided final proof of the feasibility of the methodology. Despite the ageing, the complex matrix and the micro-size of the sample, it was possible to detect and quantify casein by dot-blot immunoassay. The specific and unambiguous result makes the proposed protocol a suitable procedure to recognize aged proteins with a degraded amino acid pattern

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Section: Discussionmentioning

confidence: 99%

Sidestepping the challenge of casein quantification in ancient paintings by dot-blot immunoassay

Cattò

Gambino

Cappitelli

et al. 2017

Microchemical Journal

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“…BaO + 9 H2O → Ba (OH)2 • 8H2O. Senyawa ini mengkristal sebagai oktahidrat (49)(50)(51) yang mengkonversi menjadi monohidrat setelah pemanasan di udara, sehingga sulit untuk menentukan bagaimana kebasaan dari senyawa yang terbentuk dari elemen barium tersebut. Senyawa ini perlu untuk dikenali lagi bagaimana karakteristiknya sehingga senyawa ini tak mudah terdekomposisi menjadi senyawa lain.…”

Section: Analysis Gapunclassified

“…Rumus kimia : OH -Massa molar : 17,01 g/mol Asam konjugasi : air Basa konjugasi :anion oksida Analisis 2D Barium hidroksida (49)(50)(51) menggunakan ChemDraw Ultra. (77)…”

Section: B Ion Hidroksidaunclassified

A Review Ba(OH)2 : Transpor Ionik pada Barium Hidroksida di dalam Air dengan Konsep Termodinamika

Yanti¹,

Zainul²

2018

Preprint

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Barium hidroksida dikenal dengan nama lain yaitu air barit. Barium hidroksida merupakan kristal monoklinik yang tidak bewarna, meleleh pada suhu 78 0C, larut dalam air dan tidak larut dalam aseton. Senyawa ini biasa digunakan sebagai bahan untuk membuat sabun, penyabunan lemak, dan sintesis organik. Penelitian ini bertujuan untuk menganalis interaksi molekular dan kinetik barium hidroksida. Metode yang digunakan yaitu permodelan dengan menggunakan ChemOffice 15.0. Barium hidroksida mempunyai kelarutan 101.4 g/100 ml (100℃). Pada analisa menggunakan Chemoffice didapat panjang ikatan barium hidroksida adalah 2.620 0A, peregangan: 1.3403, torsi : 0,000, bend : 496.3657, total energi : 494.9578 kcal/mol. Barium hidroksida mempunyai kelarutan 101.4 g/100 ml (100℃). Di dalam air ion barium akan tersolfasi (terbungkus) oleh molekul air, sehingga memungkinkan terjadinya transpor ionik. Parameter yang dapat diukur dalam transpor ionik ini adalah kecepatan hanyut, bilangan transportdan gerakan ionik. Barium hidroksida mempunyai termokimia pada fase cair dengan ΔH = -944.7 kj/mol. Hal ini menunjukkan bahwa pada proses adsorpsi pada zat barium hidroksida berlangsung secara spontan pada reaksi eksoterm dengan gangguan yang kecil terhadap sistem .Viskositas dan densitas dari barium hidroksida ini masing-masingnya yaitu 1.150. 10-2 g/cm-1 dan 1.064 g/cm3.

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“…Furthermore, some pigments accelerate protein degradation in the binding media [5], and chemical reactions can take place between the present organic and inorganic materials as inorganic cations that can form strong complexes with proteins [6][7][8]. It is, then, of paramount importance to develop analytical, low invasive approaches in protein identification not only for conservation and restauration purposes, but even for recognizing the techniques of a particular artist.…”

Section: Introductionmentioning

confidence: 99%

“…After that, it was tested on proteins extracted from paint models made by mixing proteins with different pigments and submitting to artificial aging, thus mimicking easel paintings. It is known that some pigments accelerate protein degradation [5], and chemical reactions can take place between organic and inorganic materials [6][7][8] After confirmation of the applicability of fluorescent labelling with protein recovered from artificial, laboratory-made complex matrices, we tried it on microsamples taken from real easel paintings. The fluorescent labelling method was then tested on microsamples obtained from easel paintings of the Italian painter, Giorgio Marini (Florence, 1836-Castelo Branco, 1905).…”

Section: Introductionmentioning

confidence: 99%

Development of a Simple Method for Labeling and Identification of Protein Binders in Art

et al. 2019

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Easel paintings are assets with an important historic and cultural value. They usually possess a multi-tiered structure, composed of different layers some of which may present protein binders, making it important to identify these materials for restoration and conservation purposes. We propose the identification of different protein binders by a new fluorescent labeling method employing a coumarin based chromophore, C392STP (sodium(E/Z)-4-(4-(2-(6,7-dimethoxycoumarin-3-yl)vinyl)benzoyl)-2,3,5,6-tetrafluorobenzenesulfo-nate). The method was optimized using commercial proteins and was further tested on proteins extracted from hen’s egg yolk, white bovine milk, and rabbit skin glue. To model more realistic conditions, paint models of easel paintings were prepared. The paint models were made with hen’s egg yolk, white bovine milk, and rabbit skin glue, mixed with different pigments and submitted to artificial aging. Then the extracted proteins from the paint models were labeled with C392 which allowed a sensitive and selective identification by polyacrylamide gel electrophoresis (PAGE) of the different protein binders used. As a final test, three 19th century easel paintings, from the Italian painter Giorgio Marini, were analyzed. The results show the potential of the proposed method for the identification of protein binders present in easel paintings.

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Influence of pigments and protein aging on protein identification in historically representative casein-based paints using enzyme-linked immunosorbent assay

Cited by 27 publications

References 36 publications

Sidestepping the challenge of casein quantification in ancient paintings by dot-blot immunoassay

Sidestepping the challenge of casein quantification in ancient paintings by dot-blot immunoassay

A Review Ba(OH)2 : Transpor Ionik pada Barium Hidroksida di dalam Air dengan Konsep Termodinamika

Development of a Simple Method for Labeling and Identification of Protein Binders in Art

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