Lecture
Gerhard Schulze Young Talent Award 2026 Expanding the Archaeometric Toolkit: A Novel Combination of MALDI-MSI, ATR/FTIR and Raman Imaging for Parchment Degradation Studies
- at -
- ICM Saal 4a
- Type: Award
Lecture description
Antonia Malissa, Manfred Schreiner, Martina Marchetti-Deschmann
Among historic writing supports parchment holds a special position, being of animal origin. Although it has a paper-like appearance, the writing substrate is a highly engineered biomaterial produced from the skins of domestic animals, like sheep. Preparation involves extensive processing to remove the epidermal layers, leaving the dermis as a compact, fibrous arrangement rich in collagen, accompanied by lipids. Parchment documents may have undergone changes in structural stability and molecular composition over centuries due to natural aging or improper handling. The primary driving factors include types of environmental stress, such as light exposure and atmospheric pollutants. Oxidative stress proved to be particularly harmful as it induces lipid peroxidation and chemical alterations of collagen, ultimately weakening material stability and durability. Conventional spectroscopic approaches have been used to monitor these alterations by observing modifications of the protein backbone on the direct parchment surface. [1] To complement their limitations in molecular specificity, we present a comprehensive strategy that integrates lateral proteomic and lipidomic analyses with spectroscopic imaging to characterize degradation-related modifications in parchment at the fibrillar scale.
For this purpose, sheep parchment was artificially aged using controlled, accelerated light- and SO2-aging protocols. [1] Following surface measurements using ATR/FTIR and µ-Raman spectroscopy, the samples were prepared, by embedding and sectioning, for imaging analyses of the two-dimensional arrangement of horizontal layers. ATR/FTIR and Raman microspectroscopic imaging were achieved with spatial resolutions below 10 µm. Lipids and proteins were further targeted in serial sections using MALDI FTICR mass spectrometry imaging (MSI) at lateral resolutions of 15 µm. In-depth spectroscopic analyses, both in bulk and via imaging, revealed a progressive weakening of the hydrogen bond-stabilized architecture of collagen, characterized by changes in the protein secondary structures from helical conformations to β-sheets and disordered states. Spatially resolved analysis enabled the localization of these changes at subsurface levels, thereby improving the assessment of the overall parchment condition after aging. Proteomic MALDI MSI provided a previously unreported molecular and spatial overview of collagens and proteoglycans in parchment. Degradation-induced modifications of fibril- and network-forming collagens, and an increased loss of dermal proteoglycans, correlated with the decrease in hierarchical organization. Although parchment contains low lipid levels compared with intact skin, lipidomic MALDI MSI detected diverse lipid species and their oxidation products, serving as additional stress markers. By this, the study provided so far unexplored insight into degradation processes and, therefore, damage assessment of the material.
[1] Malissa, A. et al., Molecules 2023, 28, 4584.
Among historic writing supports parchment holds a special position, being of animal origin. Although it has a paper-like appearance, the writing substrate is a highly engineered biomaterial produced from the skins of domestic animals, like sheep. Preparation involves extensive processing to remove the epidermal layers, leaving the dermis as a compact, fibrous arrangement rich in collagen, accompanied by lipids. Parchment documents may have undergone changes in structural stability and molecular composition over centuries due to natural aging or improper handling. The primary driving factors include types of environmental stress, such as light exposure and atmospheric pollutants. Oxidative stress proved to be particularly harmful as it induces lipid peroxidation and chemical alterations of collagen, ultimately weakening material stability and durability. Conventional spectroscopic approaches have been used to monitor these alterations by observing modifications of the protein backbone on the direct parchment surface. [1] To complement their limitations in molecular specificity, we present a comprehensive strategy that integrates lateral proteomic and lipidomic analyses with spectroscopic imaging to characterize degradation-related modifications in parchment at the fibrillar scale.
For this purpose, sheep parchment was artificially aged using controlled, accelerated light- and SO2-aging protocols. [1] Following surface measurements using ATR/FTIR and µ-Raman spectroscopy, the samples were prepared, by embedding and sectioning, for imaging analyses of the two-dimensional arrangement of horizontal layers. ATR/FTIR and Raman microspectroscopic imaging were achieved with spatial resolutions below 10 µm. Lipids and proteins were further targeted in serial sections using MALDI FTICR mass spectrometry imaging (MSI) at lateral resolutions of 15 µm. In-depth spectroscopic analyses, both in bulk and via imaging, revealed a progressive weakening of the hydrogen bond-stabilized architecture of collagen, characterized by changes in the protein secondary structures from helical conformations to β-sheets and disordered states. Spatially resolved analysis enabled the localization of these changes at subsurface levels, thereby improving the assessment of the overall parchment condition after aging. Proteomic MALDI MSI provided a previously unreported molecular and spatial overview of collagens and proteoglycans in parchment. Degradation-induced modifications of fibril- and network-forming collagens, and an increased loss of dermal proteoglycans, correlated with the decrease in hierarchical organization. Although parchment contains low lipid levels compared with intact skin, lipidomic MALDI MSI detected diverse lipid species and their oxidation products, serving as additional stress markers. By this, the study provided so far unexplored insight into degradation processes and, therefore, damage assessment of the material.
[1] Malissa, A. et al., Molecules 2023, 28, 4584.
