Publications by authors named "Sebastian Florez-Rueda"
Article Synopsis
- The spike protein of SARS-CoV-2 attaches to the α1-helix of human ACE2, suggesting that peptides mimicking this helix could block viral entry.
- Researchers created modified peptides using a diproline module, ProM-5, to enhance their α-helical structure based on the ACE2 sequence.
- Experiments showed that while ProM-5 increased helicity, replacing non-binding amino acids with alanine significantly enhanced helicity, and one peptide was identified with strong binding affinity to the spike protein (K = 62 nM).
The pathogenic agent of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) enters into human cells through the interaction between the receptor binding domain (RBD) of its spike glycoprotein and the angiotensin-converting enzyme 2 (ACE2) receptor. Efforts have been made towards finding antivirals that block this interaction, therefore preventing infection. Here, we determined the binding affinity of ACE2-derived peptides to the RBD of SARS-CoV-2 experimentally and performed MD simulations in order to understand key characteristics of their interaction.
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