Skip to main content

News

News

Bordeaux Summer School 2021 - Advanced mass spectrometry applied to cultural heritage - June 16th-18th, 2021

Bandeau

Bordeaux Summer School - Advanced mass spectrometry applied to cultural heritage

June 16th - June 18th, 2021
 

This online summer school is an innovative and inter / multi-disciplinary training based on advanced mass spectrometry to decipher the complexity of cultural heritage material, i.e. artworks, archaeological and palaeological materials, via their organic macromolecular signatures uncoding (proteins, lipids, polysaccharides).

Lasting three days, the course is delivered remotely and combines lectures and workshops in sample preparation, current mainstream mass spectrometry techniques and their most recent improvements, omics, and bioinformatics, all within the framework of cultural heritage. The program is open to doctoral students, post-doctoral researchers, academics, as well as private and museum actors in analytical and heritage sciences.

 

Program

At this link, the latest updated version of the schedule: link.

 

Speakers

A college of pioneering researchers will present their most recent developments and achievements in the field of cultural heritage mass spectrometry, including technical and computational developments and applications.

  • Julie Arslanoglu, The Metropolitan Museum of Art, New York, USA.

  • Leila Birolo, University of Naples, Italy.

  • Ilaria Bonaduce, University of Pisa, Italy.

  • Enrico Cappellini, University of Copenhagen, Denmark.

  • Rémy Chapoulie, University Bordeaux-Montaigne, France.

  • Matthew Collins, University of Cambridge, England and University of Copenhagen, Denmark.

  • Garry Corthals, University of Amsterdam, The Netherlands.

  • Juergen Cox, Max Planck Institute of Biochemistry, Germany.

  • Francesco D’Errico, University of Bordeaux, France.

  • Nathalie Fourment, National Museum of Prehistory, France.

  • Sven Haakanson, University of Washington, Seattle, USA.

  • Katrien Keune, Rijksmuseum, Amsterdam, The Netherlands.

  • G. Asher Newsome, Smithsonian Museum Conservation Institute, Washington D.C., USA.

  • Caroline Tokarski, University of Bordeaux-CNRS, France.

 

Pratical informations

Dates: June 16th-28th, 2021.

N° participants: 20

Language: Classes, discussions and group work will be in English. Candidates should have a B2 level of English or equivalent.

Format: This summer school will be delivered via remote learning.

Participant profile: The course is designed for doctoral students, post-doctoral researchers, academics, as well as private and museum actors in analytical and heritage sciences. Knowledge in mass spectrometry (fundamentals) is required.

Applications: Candidates must provide a CV and cover letter detailing their motivation for attending the summer school and two professional references (i.e. names, emails, and addresses). Registration being limited to 20 participants, attendees will be selected by the organizing committee from the candidate pool based on merit, background, and other criteria.

Deadline: May 2nd, 2021.

Participation fee: 150 € (incl. VAT) per participant.

More information: https://bss-appliedchemistry.u-bordeaux.fr/en/

PhD defense - Francesca Galluzzi

Francesca Galluzzi
              Francesca Galluzzi

Date : Tuesday, February 23, 2021, 03:30 PM (UTC+1), auditorium of ENSTBB, Bordeaux.

Title : "New developments in high-resolution mass spectrometry for proteomic analysis applied to cultural heritage: study of intact proteins, their cross-linkages and interactions in artworks and museum objects".

Summary : Proteins in cultural heritage objects constitute a critical source of information. Their detection and characterisation can provide an accurate comprehension of the artist’s technique and formulations. A more in-depth insight of the state of conservation and history of the artwork can also be achieved through investigation at the molecular level of the degradation mechanisms induced by natural ageing, environmental factors or either by inappropriate conservation/restoration treatments. Firstly, the PhD was dedicated to the development of proteomic bottom-up and top-down strategies using mass spectrometry for the study of proteins at trace levels from historical and artistic objects. The potentialities of a combination of these two complementary approaches were highlighted in the study of Gainsborough’s drawings, where the presence of milk-based fixatives was revealed with samples collected with minimally invasive techniques. Information achieved with the peptidic analysis, such as the specific breed origin of the detected proteins and their modifications, were enriched through top-down analysis with the detection of highly modified proteoforms characterised by multiple cleavage patterns. Secondly, the PhD study aimed to achieve a better insight into the proteins’ structural and conformational alterations in an artwork. A strategy based on the elaboration of data from the bottom-up analysis was optimised to investigate the protein networks formations through the localisation and characterisation of cross-linked peptidic pairs. The methodology was initially tested on mock-ups of paintings (formulated with lysozyme mixed with lead white pigment) which were treated with oxidising agents and naturally aged. The detection of different reticulated products led to defining various molecular patterns characteristic of oxidative-based cross-links in the lysozyme protein which subsequently were detected in more complex samples from historical tempera paintings. The cross-linking examination, combined with an unbiased modification search, also was effective for a more exhaustive understanding of the conservation history of a Coptic manuscript subjected to ancient invasive restoration treatment. The detection of a great extent of lysine methylations and especially the characteristic fragmentation markers of formaldehyde-based cross-links provided the first analytical evidence of a potential parchment consolidation treatment based on gelatin-formol used by the Vatican library during restoration. The developed approach also offered a more accurate protein identification detecting peptides that passed unnoticed in the classical strategy because they were chemically modified or structurally unreachable. Finally, the action of some of the most common inorganic pigments on proteins molecular and structural changes was also investigated. Particularly, the role of these inorganic compounds in proteins conformational changes was investigated for the first time through Hydrogen/Deuterium exchange (HDX) studies via mass spectrometry (intact protein approach). The decrease of deuterium exchange observed for certain mixtures suggested the interposition of the pigment in the protein solvent accessibility, or/and the modification of the molecular conformation.

Members of the jury : 

Dr Arslanoglu Julie, Department of Scientific Research, The Metropolitan Museum of Art, USA.
Professor Birolo Leila, University of Naples Federico II, Italy.
Professor associate Bonaduce Ilaria, University of Pisa, Italy.
Professor Chapoulie Rémy, University of Bordeaux Montaigne, France.
Professor Collins Matthew, University of Copenhagen, Denmark.
Dr Dufourc Erick, Centre National de la Recherche Scientifique, Bordeaux, France.
Dr Menu Michel, Centre de Recherche et de Restauration des Musées de France, France.
Professor Tokarski Caroline, University of Bordeaux, France.

Information of the PhD : The doctoral project of Galluzzi Francesca has been supported by the Marie Skłodowska‐Curie European Training Network (ETN) “TEMPERA” for paleoproteomic analysis of cultural heritage (http://www.tempera-etn.eu). The project focused on mass spectrometry-based ancient protein residues analysis for biomolecular diagnostics and conservation of cultural heritage material.

PhD defense - Fatima Zahra Alem

Fatima Zahra Alem
           Fatima Zahra Alem

Date : Friday, February 19th, 2021, 2:00 PM (UTC+1), Salle de conferences, CGFB, Bordeaux.

Title : "Extraction and analysis by liquid chromatography coupled with mass spectrometry of Lawsonia inermis and the study of its anti-melanoma effect".

Summary : Lawsonia inermis L. commonly called Henna belongs to the family Lythraceae. It is known for its traditional importance both as a cosmetic and medicinal agent, especially in the indigenous regions of North Africa, South Asia and Middle East countries. The different parts of this shrub; leaves, stems, seeds and roots have different chemical constituents such as naphthoquinones, polyphenols, flavonoids, tannins, etc, which have various biological activities. The interest of this Mediterranean plant, in addition to its cosmetic use, is its biological activity antimicrobial, anti-inflammatory, anticancer and many others. This research work has been particularly interested in studying its anticancerous effect and more particularly its potential anti-melanoma metastasis given its traditional use often as a topical treatment for irritated skin. This research work allowed, first of all, the development of an experimental plan for the optimization of the global yield of extraction of active molecules from Henna (Lawsonia inermis L.). In the second stage, the identification and quantification of active compounds by high performance liquid chromatography coupled with mass spectrometry.  A geographical mapping of henna crops in southern Morocco, using principal component analysis and based on the nature of the climate of each region was carried out. Subsequently, the effect of plumbagin on metastatic melanoma was studied. The study of this activity was evaluated in-vitro on murine and human cells respectively B16F10 and SKMEL-28. Plumbagin was found to significantly inhibit three important metastatic processes: migration, adhesion and invasion of B16F10 cells. These results were confirmed in the human cell line SK-MEL-28.

Keywords : Lawsonia inermis, naphthoquinones, extraction, HPLC, mass spectrometry, melanoma

Members of the jury : 

Pr. Catia Contado, University of Ferrara, Italy - Reporter
Pr. Amaral Joana Soares, Polytechnic Institute of Bragança, Portugal - Reporter
Pr. Abdelaziz Benjouad, University of Rabat, Morocco - External examiner
Pr. Eddouks Mohammed, University Moulay Ismail - Meknès, Morocco - External examiner
Pr. Rabii Ameziane Hassani, University Mohamed V, Morocco - Internal examiner
Pr. Waffo-Teguo Pierre, University of Bordeaux, France - Internal examiner
Pr. Isoda Hiroko, University of Tsukuba, Japan - Guest member 
Pr. Mayra O.Villareal, University of Tsukuba, Japan - Guest member
Pr. Nadia Dakka, University Mohamed V, Morocco - Guest member
Pr. Zoubida Charrouf, University Mohamed V, Morocco - Guest member
Pr. Boutayna Rhourri-Frih, University of Bordeaux, France - Thesis Director
Pr. Youssef Bakri, University Mohamed V, Morocco - Thesis Director

Information of the PhD : This PhD project is a joint program between Bordeaux University in France and Mohamed V University in Morocco, and a collaboration with Isoda Lab in Tsukuba University, Japan under the supervision of Pr Isoda Hiroko. The doctoral project has been financially supported by the excellence doctoral scholarship EIFFEL from French government and Japan Student Services Organization (JASSO) from Japan.

Invitation to review in Analytical Chemistry

Nicolas Desbenoit from the Biological Mass Spectrometry team was invited as expert by the journal "Analytical Chemistry" to write a review in the field of multimodal imaging combining vibrational spectroscopies and mass spectrometry imaging applied to any biological samples. This review is meant as an introduction for experts in MSI to become acquainted with vibrational spectroscopies and vice versa.

Molecular imaging has the potential to unearth important spatial and temporal relationships in biological systems, including intercellular signaling as well as environmentally-cued morphological changes. Various chemical imaging techniques show functional groups, molecular weights, etc. but no individual technique to date has the ability to simultaneously access all chemical information. Thus, it is highly attractive to combine information from two or more analytical techniques. Multimodal imaging is a recent, highly effective strategy for acquiring images by combining chemical information from multiplexed platforms. This emerging integrated imaging approach yields information unattainable from a single method, enabling the evaluation of subtle biochemical changes and opening the way for a quantitative molecular overview of the morphological structure in biological tissues or architecture of cells. As a result, qualitative and quantitative multi-omics investigations have the capability to revolutionize our understanding of disease progression and the healing process. Such a strategy has received increasing attention as it helps to elucidate the complex spatial distribution of biomolecules from the surface of a biological sample while circumventing the specific limitations of an individual imaging technique.

Because multimodal imaging constitutes a vast subject area, emphasis is placed on the well-established vibrational spectroscopies including Fourier transform infra-red (FTIR) and confocal Raman microscopy (CRM), as well as mass spectrometry imaging (MSI), namely time-of-flight secondary ion mass spectrometry (ToF-SIMS), and matrix-assisted laser desorption/ionization (MALDI).
 

Reference : Tuck M, Blanc L, Touti R, Patterson NH, Van Nuffel S, Villette S, Taveau JC, Römpp A, Brunelle A, Lecomte S, Desbenoit N. Multimodal Imaging Based on Vibrational Spectroscopies and Mass Spectrometry Imaging Applied to Biological Tissue: A Multiscale and Multiomics Review. Anal Chem. 2021 Jan 12;93(1):445-477. [PubMed]

Contact : Nicolas Desbenoit, CNRS Researcher, University of Bordeaux.
n.desbenoit@cbmn.u-bordeaux.fr

New partnership with the University of Montréal

Université de Montréal
                   Université de Montréal

From September 2021, Dr Boutayna Rhourri Frih, associate professor at the school of Pharmaceutical Sciences at the University of Bordeaux and researcher in the mass spectrometry team led by Caroline Tokarski at the CBMN, will join the Professor Pierre Chaurand, laboratory of molecular imaging, as a visiting professor for a period of three years. Boutayna intends to continue the development of molecular imaging methodologies related to public health issues, in particular with the study of the comorbidity of heart failure and viral infection (COVID-19), or the study of triple negative breast cancer and analysis of brain lipidome in Parkinson's disease. This delegation to the University of Montreal will help to set up new collaborations and exchange opportunities both in terms of research and teaching.


Contact : Boutayna Rhourri Frih

Link : https://www.linkedin.com/in/boutaynarhourrifrih/