A versatile and user-friendly approach for the analysis of proteins in ancient and historical objects

Ntasi, Georgia; Kirby, Daniel P.; Stanzione, Ilaria; Carpentieri, Andrea; Somma, Maria Patrizia; Cicatiello, Paola; Marino, Gennaro; Giardina, Paola; Birolo, Leila

doi:10.1016/j.jprot.2020.104039

Cited by 17 publications

(10 citation statements)

References 25 publications

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“…In cases where the proportion or preservation of binder proteins is very low, targeting techniques such as MRM can help improve the detection of binder peptides, and this has proven particularly useful for identifying egg proteins in cases where their presence was suspected but not previously detected . The recent development of low cost, minimally destructive sampling techniques that can be conducted without specialist training ,,,,− promises to make proteomic studies of artwork more feasible, and further development of PMF using MALDI-TOF will facilitate larger scale data collection.…”

Section: Applications In Paleoproteomicsmentioning

confidence: 99%

Paleoproteomics

2022

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Paleoproteomics, the study of ancient proteins, is a rapidly growing field at the intersection of molecular biology, paleontology, archaeology, paleoecology, and history. Paleoproteomics research leverages the longevity and diversity of proteins to explore fundamental questions about the past. While its origins predate the characterization of DNA, it was only with the advent of soft ionization mass spectrometry that the study of ancient proteins became truly feasible. Technological gains over the past 20 years have allowed increasing opportunities to better understand preservation, degradation, and recovery of the rich bioarchive of ancient proteins found in the archaeological and paleontological records. Growing from a handful of studies in the 1990s on individual highly abundant ancient proteins, paleoproteomics today is an expanding field with diverse applications ranging from the taxonomic identification of highly fragmented bones and shells and the phylogenetic resolution of extinct species to the exploration of past cuisines from dental calculus and pottery food crusts and the characterization of past diseases. More broadly, these studies have opened new doors in understanding past human−animal interactions, the reconstruction of past environments and environmental changes, the expansion of the hominin fossil record through large scale screening of nondiagnostic bone fragments, and the phylogenetic resolution of the vertebrate fossil record. Even with these advances, much of the ancient proteomic record still remains unexplored. Here we provide an overview of the history of the field, a summary of the major methods and applications currently in use, and a critical evaluation of current challenges. We conclude by looking to the future, for which innovative solutions and emerging technology will play an important role in enabling us to access the still unexplored "dark" proteome, allowing for a fuller understanding of the role ancient proteins can play in the interpretation of the past.

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Section: Applications In Paleoproteomicsmentioning

confidence: 99%

Paleoproteomics

2022

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“…The released peptides are captured onto the film surface and then analyzed when required, by a simple MALDI-TOF analysis or, eventually, by more resolutive and informative LC–MS/MS analyses ( Cicatiello et al, 2018 ). Additionally, this lab-on-plate method was implemented immobilizing the glycosidases PNGaseF on the Vmh2-coated sheet for a two-step procedure in which the deglycosylation pretreatment allows an improved proteolysis and detection of glycosylated proteins ( Ntasi et al, 2021 ).…”

Section: Protein Structure Analysis and Proteomic Applicationsmentioning

confidence: 99%

Innovative surface bio-functionalization by fungal hydrophobins and their engineered variants

Stanzione

Pitocchi

Pennacchio

et al. 2022

Front. Mol. Biosci.

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Research on innovative surface functionalization strategies to develop materials with high added value is particularly challenging since this process is a crucial step in a wide range of fields (i.e., biomedical, biosensing, and food packaging). Up to now, the main applied derivatization methods require hazardous and poorly biocompatible reagents, harsh conditions of temperature and pressure, and are time consuming and cost effective. The discovery of biomolecules able to adhere by non-covalent bonds on several surfaces paves the way for their employment as a replacement of chemical processes. A simple, fast, and environment-friendly method of achieving modification of chemically inert surfaces is offered by hydrophobins, small amphiphilic proteins produced by filamentous fungi. Due to their structural characteristics, they form stable protein layers at interfaces, serving as anchoring points that can strongly bind molecules of interest. In addition, genetic engineering techniques allow the production of hydrophobins fused to a wide spectrum of relevant proteins, providing further benefits in term of time and ease of the process. In fact, it is possible to bio-functionalize materials by simply dip-casting, or by direct deposition, rendering them exploitable, for example, in the development of biomedical and biosensing platforms.

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“…Indeed, although modern high-performance mass spectrometers require very low amounts of sample, most of the actual protocols of analyses remain invasive, requiring the destruction of part of the ancient items under study; a practice that is (obviously) discouraged by most museums. Consequently, during the last decade, different minimally invasive methods have been developed to harvest and investigate ancient samples. − A promising non-invasive technique, which at present appears to allow full exploration of any item in the Cultural Heritage arena without any damage or contamination, is known under the acronym EVA (ethylene-vinyl acetate) . It consists of a plastic film of ethylene-vinyl acetate studded with strong cation and anion exchangers as well as with C18 and C8 hydrophobic resins which, when applied to any type of surface, is able to extract proteins and small molecules.…”

Section: Introductionmentioning

confidence: 99%

Count Dracula Resurrected: Proteomic Analysis of Vlad III the Impaler’s Documents by EVA Technology and Mass Spectrometry

Pittalà,

Di Francesco,

Cucina

et al. 2023

Anal. Chem.

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The interest of scientists in analyzing items of World Cultural Heritage has been exponentially increasing since the beginning of the new millennium. These studies have grown considerably in tandem with the development and use of sophisticated and sensitive technologies such as high-resolution mass spectrometry (MS) and the non-invasive and non-damaging technique, known under the acronym EVA (ethylene-vinyl acetate). Here, we report the results of the MS characterization of the peptides and proteins harvested by the EVA technology applied to three letters written in 1457 and 1475 by the voivode of Wallachia, Vlad III, also known as Vlad the Impaler, or Vlad Dracula. The discrimination of the "original" endogenous peptides from contaminant ones was obtained by monitoring their different levels of deamidation and of other diagenetic chemical modifications. The characterization of the ancient proteins extracted from these documents allowed us to explore the environmental conditions, in the second half of the 15th century, of the Wallachia, a region considered as a meeting point for soldiers, migrants, and travelers that probably carried not only trade goods and cultural traditions but also diseases and epidemics. In addition, the identification of many human peptides and proteins harvested from the letters allowed us to uncover more about Vlad Dracula the Impaler. Particularly, the experimental data show that he probably suffered from inflammatory processes of the respiratory tract and/or of the skin. In addition, proteomics data, although not exhaustive, suggest that, according to some stories, he might also have suffered from a pathological condition called hemolacria, that is, he could shed tears admixed with blood. It is worth noting that more medieval people may have touched these documents, which cannot be denied, but it is also presumable that the most prominent ancient proteins should be related to Prince Vlad the Impaler, who wrote and signed these letters. The data have been deposited to the ProteomeXchange with the identifier ⟨PXD041350⟩.

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A versatile and user-friendly approach for the analysis of proteins in ancient and historical objects

Cited by 17 publications

References 25 publications

Paleoproteomics

Paleoproteomics

Innovative surface bio-functionalization by fungal hydrophobins and their engineered variants

Count Dracula Resurrected: Proteomic Analysis of Vlad III the Impaler’s Documents by EVA Technology and Mass Spectrometry

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