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

Bibliographic Details
Title: Infrared Spectroscopy of SARS‐CoV‐2 Viral Protein: from Receptor Binding Domain to Spike Protein
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
More Details
ISSN:21983844
20240082
DOI:10.1002/advs.202400823
Published in:Advanced Science
Language:English