Spike (S) glycoprotein is the largest structural protein of SARS-CoV-2 virus and the main one involved in anchoring of the host receptor ACE2 through the receptor binding domain (RBD). S protein secondary structure is of great interest for shedding light on various aspects, from functionality to pathogenesis, finally to spectral fingerprint for the design of optical biosensors. In this paper, the secondary structure of SARS-CoV-2 S protein and its constituting components, namely RBD, S1 and S2 regions, are investigated at serological pH by measuring their amide I infrared absorption bands through Attenuated Total Reflection Infrared (ATR-IR) spectroscopy. Experimental data in combination with MultiFOLD predictions, Define Secondary Structure of Proteins (DSSP) web server and Gravy value calculations, provide a comprehensive understanding of RBD, S1, S2, and S proteins in terms of their secondary structure content, conformational order, and interaction with the solvent.

Mancini, T., Macis, S., Mosetti, R., Luchetti, N., Minicozzi, V., Notargiacomo, A., et al. (2024). Infrared Spectroscopy of SARS-CoV-2 Viral Protein: from Receptor Binding Domain to Spike Protein. ADVANCED SCIENCE [10.1002/advs.202400823].

Infrared Spectroscopy of SARS-CoV-2 Viral Protein: from Receptor Binding Domain to Spike Protein

Minicozzi V.;
2024-01-01

Abstract

Spike (S) glycoprotein is the largest structural protein of SARS-CoV-2 virus and the main one involved in anchoring of the host receptor ACE2 through the receptor binding domain (RBD). S protein secondary structure is of great interest for shedding light on various aspects, from functionality to pathogenesis, finally to spectral fingerprint for the design of optical biosensors. In this paper, the secondary structure of SARS-CoV-2 S protein and its constituting components, namely RBD, S1 and S2 regions, are investigated at serological pH by measuring their amide I infrared absorption bands through Attenuated Total Reflection Infrared (ATR-IR) spectroscopy. Experimental data in combination with MultiFOLD predictions, Define Secondary Structure of Proteins (DSSP) web server and Gravy value calculations, provide a comprehensive understanding of RBD, S1, S2, and S proteins in terms of their secondary structure content, conformational order, and interaction with the solvent.
2024
Online ahead of print
Rilevanza internazionale
Articolo
Esperti anonimi
Settore FIS/07
English
Con Impact Factor ISI
ATR‐IR spectroscopy
MultiFOLD
Spike glycoproteins
hydrophobicity
secondary structure
Mancini, T., Macis, S., Mosetti, R., Luchetti, N., Minicozzi, V., Notargiacomo, A., et al. (2024). Infrared Spectroscopy of SARS-CoV-2 Viral Protein: from Receptor Binding Domain to Spike Protein. ADVANCED SCIENCE [10.1002/advs.202400823].
Mancini, T; Macis, S; Mosetti, R; Luchetti, N; Minicozzi, V; Notargiacomo, A; Pea, M; Marcelli, A; Ventura, Gd; Lupi, S; D'Arco, A
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/375483
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