Infrared Spectroscopy of SARS‐CoV‐2 Viral Protein: from Receptor Binding Domain to Spike Protein
Title: | Infrared Spectroscopy of SARS‐CoV‐2 Viral Protein: from Receptor Binding Domain to Spike Protein |
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Authors: | Tiziana Mancini, Salvatore Macis, Rosanna Mosetti, Nicole Luchetti, Velia Minicozzi, Andrea Notargiacomo, Marialilia Pea, Augusto Marcelli, Giancarlo Della Ventura, Stefano Lupi, Annalisa D'Arco |
Source: | Advanced Science, Vol 11, Iss 39, Pp n/a-n/a (2024) |
Publisher Information: | Wiley, 2024. |
Publication Year: | 2024 |
Collection: | LCC:Science |
Subject Terms: | ATR‐IR spectroscopy, hydrophobicity, MultiFOLD, secondary structure, Spike glycoproteins, Science |
More Details: | 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. |
Document Type: | article |
File Description: | electronic resource |
Language: | English |
ISSN: | 2198-3844 20240082 |
Relation: | https://doaj.org/toc/2198-3844 |
DOI: | 10.1002/advs.202400823 |
Access URL: | https://doaj.org/article/a16260a4763643139b41a1892eec1e6f |
Accession Number: | edsdoj.16260a4763643139b41a1892eec1e6f |
Database: | Directory of Open Access Journals |
ISSN: | 21983844 20240082 |
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DOI: | 10.1002/advs.202400823 |
Published in: | Advanced Science |
Language: | English |