Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1.
Maryann MoralesRaheleh RavanfarPaul H OyalaHarry B GrayJay R WinklerPublished in: Inorganic chemistry (2022)
The first encoded SARS-CoV-2 protein (Nsp1) binds to the human 40S ribosome and blocks synthesis of host proteins, thereby inhibiting critical elements of the innate immune response. The final 33 residues of the natively unstructured Nsp1 C-terminus adopt a helix-turn-helix geometry upon binding to the ribosome. We have characterized the fluctuating conformations of this peptide using circular dichroism spectroscopy along with measurements of tryptophan fluorescence and energy transfer. Tryptophan fluorescence decay kinetics reveal that copper(II) binds to the peptide at micromolar concentrations, and electron paramagnetic resonance spectroscopy indicates that the metal ion coordinates to the lone histidine residue.
Keyphrases
- energy transfer
- sars cov
- immune response
- quantum dots
- single molecule
- respiratory syndrome coronavirus
- high resolution
- endothelial cells
- escherichia coli
- staphylococcus aureus
- pseudomonas aeruginosa
- signaling pathway
- sensitive detection
- living cells
- biofilm formation
- dendritic cells
- antimicrobial resistance
- amino acid
- protein protein
- induced pluripotent stem cells
- pluripotent stem cells
- dna methylation
- fluorescent probe
- transcription factor
- candida albicans