Accurate identification and characterization of allergenic proteins at the molecular level are essential for pinpointing the specific protein structures responsible for allergic reactions, thus advancing the development of precise diagnostic tests. Significant efforts have been focused on novel experimental techniques aimed at deepening the understanding of the underlying molecular mechanisms of these reactions. In this work, we show, for the first time to our knowledge, the unique Raman fingerprint of three Parietaria judaica (Par j) allergenic proteins. These proteins are typically present in pollen and are known to trigger severe respiratory diseases. In our research, we further exploited the surface-enhanced Raman scattering (SERS) effect from an Ag dendrite substrate. This approach provided better discrimination and a comprehensive analysis of the proteins Par j 1, 2, and 4 in hydration conditions, enabling rapid differentiation between them through a spectroscopic study.
First Vibrational Fingerprint of Parietaria judaica Protein via Surface-Enhanced Raman Spectroscopy
Morganti D.;Longo V.;Leonardi A. A.;Irrera A.;Colombo P.;Fazio B.
2025
Abstract
Accurate identification and characterization of allergenic proteins at the molecular level are essential for pinpointing the specific protein structures responsible for allergic reactions, thus advancing the development of precise diagnostic tests. Significant efforts have been focused on novel experimental techniques aimed at deepening the understanding of the underlying molecular mechanisms of these reactions. In this work, we show, for the first time to our knowledge, the unique Raman fingerprint of three Parietaria judaica (Par j) allergenic proteins. These proteins are typically present in pollen and are known to trigger severe respiratory diseases. In our research, we further exploited the surface-enhanced Raman scattering (SERS) effect from an Ag dendrite substrate. This approach provided better discrimination and a comprehensive analysis of the proteins Par j 1, 2, and 4 in hydration conditions, enabling rapid differentiation between them through a spectroscopic study.| File | Dimensione | Formato | |
|---|---|---|---|
|
biosensors-15-00182.pdf
accesso aperto
Licenza:
Dominio pubblico
Dimensione
3.54 MB
Formato
Adobe PDF
|
3.54 MB | Adobe PDF | Visualizza/Apri |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.


