Infrared Spectroscopy of SARS-CoV-2 Viral Protein: from Receptor Binding Domain to Spike Protein.
Tiziana ManciniSalvatore MacisRosanna MosettiNicole LuchettiVelia MinicozziAndrea NotargiacomoMarialilia PeaAugusto MarcelliGiancarlo Della VenturaStefano LupiAnnalisa D'ArcoPublished in: Advanced science (Weinheim, Baden-Wurttemberg, Germany) (2024)
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.
Keyphrases
- sars cov
- binding protein
- protein protein
- respiratory syndrome coronavirus
- high resolution
- molecular dynamics
- computed tomography
- small molecule
- magnetic resonance imaging
- magnetic resonance
- angiotensin ii
- transcription factor
- optical coherence tomography
- artificial intelligence
- electronic health record
- density functional theory
- ionic liquid
- high speed