Submission Type
Poster
Abstract
The RBD (Receptor Binding Domain) of spike protein (s-protein) in SARS-CoV-2 virus is highly associated with priming the viral infection, where N-terminal helices and its adjacent loop of ACE2 (Angiotensin Converting Enzyme 2) is bound to s-protein. We investigated a protein corona formation of s-protein over gold nano-colloids and reversible aggregation process as a function of pH change between acidic condition (i.e., pH ~3) and basic condition (i.e., pH ~11). The s-protein exhibited signs of aggregation through the unfolded conformation of RBD segments at the acidic condition. As the pH was repeatedly cycled between acidic and basic conditions, the aggregation was found to be quasi-reversible. The addition of ACE2 to the s-protein coated gold colloids showed two time-dependent reversible aggregation phenomena. The SERS (Surface Enhanced Raman Scattering) imaging was attempted to study s-protein adsorbed over nano-gold colloids under the presence of ACE2, and clear gold aggregates formations were observed. A significant number of those aggregates exhibited the sections which possessed repetitive localized motion at pH ~3. A preliminary study indicated there are three major Raman shifts: (1) ~1531 cm –1 : CH 2 deformation and COO – stretching of Tryptophan,(2) ~1585 cm –1 : C=C bending of phenylalanine , aromatic ring vibration, NH deformation, and (3) 2130 cm –1 : -C≡C-stretching of alkyne. The more detailed investigation of and aggregation process of s-protein coated gold and the role of ACE2 is in progress.
Recommended Citation
Tabei, Mitsuki and Boboeski, Nathan, "231 - Investigation of ACE 2 on SARS-CoV-2 spike protein coated gold colloids" (2025). GREAT Day Posters. 71.
https://knightscholar.geneseo.edu/great-day-symposium/great-day-2025/posters-2025/71
231 - Investigation of ACE 2 on SARS-CoV-2 spike protein coated gold colloids
The RBD (Receptor Binding Domain) of spike protein (s-protein) in SARS-CoV-2 virus is highly associated with priming the viral infection, where N-terminal helices and its adjacent loop of ACE2 (Angiotensin Converting Enzyme 2) is bound to s-protein. We investigated a protein corona formation of s-protein over gold nano-colloids and reversible aggregation process as a function of pH change between acidic condition (i.e., pH ~3) and basic condition (i.e., pH ~11). The s-protein exhibited signs of aggregation through the unfolded conformation of RBD segments at the acidic condition. As the pH was repeatedly cycled between acidic and basic conditions, the aggregation was found to be quasi-reversible. The addition of ACE2 to the s-protein coated gold colloids showed two time-dependent reversible aggregation phenomena. The SERS (Surface Enhanced Raman Scattering) imaging was attempted to study s-protein adsorbed over nano-gold colloids under the presence of ACE2, and clear gold aggregates formations were observed. A significant number of those aggregates exhibited the sections which possessed repetitive localized motion at pH ~3. A preliminary study indicated there are three major Raman shifts: (1) ~1531 cm –1 : CH 2 deformation and COO – stretching of Tryptophan,(2) ~1585 cm –1 : C=C bending of phenylalanine , aromatic ring vibration, NH deformation, and (3) 2130 cm –1 : -C≡C-stretching of alkyne. The more detailed investigation of and aggregation process of s-protein coated gold and the role of ACE2 is in progress.
Comments
Sponsored by Kazushige Yokoyama