SARS-CoV-2 spike binding to ACE2 is stronger and longer ranged due to glycan interaction
Yihan Huang, Bradley Harris, Shiaki A. Minami, Seongwon Jung, Priya S. Shah, Somen Nandi, Karen A. McDonald, Roland Faller
Abstract
Highly detailed steered molecular dynamics simulations are performed on differently glycosylated receptor binding domains of the severe acute respiratory syndrome coronavirus-2 spike protein. The binding strength and the binding range increase with glycosylation. The interaction energy rises very quickly when pulling the proteins apart and only slowly drops at larger distances. We see a catch-slip-type behavior whereby interactions during pulling break and are taken over by new interactions forming. The dominant interaction mode is hydrogen bonds, but Lennard-Jones and electrostatic interactions are relevant as well.
Topics & Concepts
Molecular dynamicsHydrogen bondBinding energyBiophysicsGlycanSpike ProteinChemistryInteraction energySevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Spike (software development)GlycosylationSlip (aerodynamics)CoronavirusChemical physicsCoronavirus disease 2019 (COVID-19)PhysicsBiologyComputational chemistryMoleculeBiochemistryAtomic physicsComputer scienceGlycoproteinMedicineThermodynamicsSoftware engineeringOrganic chemistryPathologyDiseaseInfectious disease (medical specialty)Protein Structure and DynamicsBacteriophages and microbial interactionsSARS-CoV-2 and COVID-19 Research