Your browser doesn't support javascript.
Show: 20 | 50 | 100
Results 1 - 2 de 2
J Phys Chem Lett ; 13(45): 10642-10648, 2022 Nov 17.
Article in English | MEDLINE | ID: covidwho-2122924


The neurological symptoms of long COVID and viral neuroinvasion have raised concerns about the potential interactions between SARS-CoV-2 protein segments and neuronal proteins, which might confer a risk of post-infection neurodegeneration, but the underlying mechanisms remain unclear. Here, we reported that the receptor-binding domain (RBD) of the spike protein and the nine-residue segment (SK9) of the envelope protein could bind to α-synuclein (αSyn) with Kd values of 503 ± 24 nM and 12.7 ± 1.6 µM, respectively. RBD could inhibit αSyn fibrillization by blocking the non-amyloid-ß component region and mediating its antiparallel ß-sheet structural conversions. Omicron-RBD (BA.5) was shown to have a slightly stronger affinity for αSyn (Kd = 235 ± 10 nM), which implies similar effects, whereas SK9 may bind to the C-terminus which accelerates the formation of parallel ß-sheet-containing oligomers and abruptly increases the rate of membrane disruption by 213%. Our results provide plausible molecular insights into the impact of SARS-CoV-2 post-infection and the oligomerization propensity of αSyn that is associated with Parkinson's disease.

COVID-19 , Coronavirus Envelope Proteins , Parkinson Disease , Spike Glycoprotein, Coronavirus , alpha-Synuclein , Humans , alpha-Synuclein/metabolism , Parkinson Disease/metabolism , Protein Binding , SARS-CoV-2 , Spike Glycoprotein, Coronavirus/metabolism , Coronavirus Envelope Proteins/metabolism
Chem Commun (Camb) ; 57(57): 6979-6982, 2021 Jul 15.
Article in English | MEDLINE | ID: covidwho-1287828


The infection of coronavirus initiates with the binding between its spike protein receptor binding domain (RBD) and a human cellular receptor called angiotensin-converting enzyme 2 (ACE2). Here, we construct truncated ACE2 peptide-conjugated gold nanoparticles as antiviral scaffolds and study their binding with the SARS-CoV-2 RBD using dynamic light scattering (DLS). Systematic DLS analysis identifies the effective peptide-nanoparticle conjugation and its efficient, specific, and long-lasting multivalent binding towards the RBD with a binding affinity of 41 nM, indicating the potential of this antiviral platform to compete with natural ACE2-RBD interactions for viral blocking and showcasing an accessible approach to measure the binding constants and kinetics.

Angiotensin-Converting Enzyme 2/chemistry , Nanoparticles/chemistry , Peptide Fragments/chemistry , Peptide Fragments/metabolism , SARS-CoV-2 , Spike Glycoprotein, Coronavirus/chemistry , Spike Glycoprotein, Coronavirus/metabolism , Dynamic Light Scattering , Molecular Dynamics Simulation , Protein Binding , Protein Domains , Substrate Specificity