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Synergetic Interaction of Writing Materials

Synergetic Interaction of Writing Materials

Federica Cappa (ORCID: 0000-0001-5591-4844)
  • Grant DOI 10.55776/P35484
  • Funding program Principal Investigator Projects
  • Status ended
  • Start October 1, 2022
  • End November 30, 2025
  • Funding amount € 292,807
  • Project website

Disciplines

Chemistry (100%)

Keywords

    Collagen, Degradation, EPR, Spectroscopy, Ageing,

Abstract

When studying the evolution of books from ancient times until the present, it is important to be aware of the simultaneous development of not only the text and its meaning, but also the different techniques and materials used through the ages. From approximately the 3rd century AC until the end of the Medieval Ages, when printing on paper was first introduced, manuscripts, scrolls, and book covers were manufactured using parchment, a material derived from animal skin, primarily sheep, calf, or goat. The main constituent of parchment is collagen, a protein with a triple-helix structure. Depending on the environmental conditions under which the medieval manuscripts are presented or stored (e.g., temperature, relative humidity, acidifying gases in the ambient atmosphere, and light), and depending on the composition of inks and pigments applied in the text and for the colorful miniatures (also called illuminations), collagen can undergo several degradation phenomena. These processes weaken the parchment structure, rendering it fragile and brittle. Moreover, they can induce a dark brown discoloration of the pigmented area, followed by mechanical damage (cracks), and, finally, loss of material (formation of holes). To study these phenomena, mock-ups of parchment, inks, and the combination of the two, will be prepared solely by following medieval recipes and procedures, using traditional materials (e.g. natural oak galls for the inks), to simulate original objects as closely as possible. In this way, it will be possible to reproduce medieval manuscripts, undergoing laboratory- controlled accelerated aging to simulate the effect of time on the objects and therefore their deterioration pathways. This will allow not only the identification of the deterioration factors but also to reconstruct the causes and chemical processes occurring during the aging. The combination of non- invasive analyses performed by compound-specific analytical methods such as Fourier Transform Infrared (FTIR) and Raman spectroscopy, as well as micro-invasive high sensitivity techniques such as Electron Paramagnetic Resonance (EPR) spectroscopy, are powerful tools for the investigation of deterioration processes occurring in proteinaceous materials. This strategy will allow not only to gain information about the deterioration phenomena found on the surface of the material but will also enhance the understanding of the chemical (deterioration) processes occurring deeper within the material. Following this approach, the complementarity of the information obtained will help to detect and identify the most relevant aging phenomena. It will therefore contribute to a more precise evaluation of the deterioration status of an object, to ensure a more effective and precise conservation strategy.

Research institution(s)
  • Akademie der bildenden Künste Wien - 100%
Project participants
  • Marc Pignitter, Universität Wien , national collaboration partner
International project participants
  • Alfonso Zoleo, Università degli studi di Padova - Italy

Research Output

  • 4 Citations
  • 2 Publications
Publications
  • 2025
    Title A Systematic Multianalytical Approach in the Study of Iron–Polyphenolic Complexes in Iron-Gall Inks: Exploring the Potentialities of Raman and Electron Paramagnetic Resonance
    DOI 10.1021/acs.inorgchem.4c04232
    Type Journal Article
    Author Caterino S
    Journal Inorganic Chemistry
    Pages 4802-4816
  • 2025
    Title Non-destructive analyses of iron-polyphenolic complexes for reconstructing iron-gall inks historical recipes
    DOI 10.1038/s40494-025-01946-x
    Type Journal Article
    Author Caterino S
    Journal npj Heritage Science
    Pages 371
    Link Publication

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