Engineered Protein Inhibitors of SARS-CoV-2 Entry: Difference between revisions

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<StructureSection load='7jzl' size='350' frame='true' side='right' caption='SARS-CoV-2 Spike Protein (7JZL):SARS-CoV-2 Spike Protein (7JZL): A trimer responsible for interacting with host ACE2 receptors to deliver the virus into host cells. Receptor binding domains (RBDs) are highlighted at the top of each monomer.' scene='10/1078124/Spike_protein/1'>
<StructureSection load='7jzl' size='350' frame='true' side='right' caption='SARS-CoV-2 Spike Protein ([[7jzl]]):SARS-CoV-2 Spike Protein ([[7jzl]]): A trimer responsible for interacting with host ACE2 receptors to deliver the virus into host cells. Receptor binding domains (RBDs) are highlighted at the top of each monomer.' scene='10/1078124/Spike_protein/1'>


==Introduction==
==Introduction==
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===Stability===
===Stability===
One of the most important findings with these De Novo proteins is their high stability, allowing for less delicate forms of administration. Additionally, it was found that the Rosetta built minibinder had a lower thermal stability than the completely De Novo proteins. Looking at the <scene name='10/1078124/Ahb2_internal_stability/1'>nonpolar core of AHB2</scene>, there are only 4 key internal residues significantly contributing to stability, and they are not oriented directly towards the center of the protein for optimal interaction. Comparatively, the <scene name='10/1078124/Lcb1_internal_stability/1'>nonpolar core of LCB1</scene> and <scene name='10/1078124/Lcb3_internal_stability/1'>LCB3</scene> had 5 key internal residues more centrally directed contributing to stability<ref name="Cao">DOI:10.1126/science.abd9909</ref>.
One of the most important findings with these De Novo proteins is their high stability, allowing for less delicate forms of administration. Additionally, it was found that the Rosetta built minibinder had a lower [https://en.wikipedia.org/wiki/Thermal_shift_assay thermal stability] than the completely De Novo proteins. Looking at the <scene name='10/1078124/Ahb2_internal_stability/1'>nonpolar core of AHB2</scene>, there are only 4 key internal residues significantly contributing to stability, and they are not oriented directly towards the center of the protein for optimal interaction. Comparatively, the <scene name='10/1078124/Lcb1_internal_stability/1'>nonpolar core of LCB1</scene> and <scene name='10/1078124/Lcb3_internal_stability/1'>LCB3</scene> had 5 key internal residues more centrally directed contributing to stability<ref name="Cao">DOI:10.1126/science.abd9909</ref>.