TY  - JOUR
A1  - Kruse, Marlen
A1  - Altattan, Basma
A1  - Laux, Eva-Maria
A1  - Grasse, Nico
A1  - Heinig, Lars
A1  - Möser, Christin
A1  - Smith, David M.
A1  - Hölzel, Ralph
T1  - Characterization of binding interactions of SARS-CoV-2 spike protein and DNA-peptide nanostructures
JF  - Scientific reports
N2  - Binding interactions of the spike proteins of the severe acute respiratory syndrome corona virus 2 (SARS-CoV-2) to a peptide fragment derived from the human angiotensin converting enzyme 2 (hACE2) receptor are investigated. 
The peptide is employed as capture moiety in enzyme linked immunosorbent assays (ELISA) and quantitative binding interaction measurements that are based on fluorescence proximity sensing (switchSENSE). 
In both techniques, the peptide is presented on an oligovalent DNA nanostructure, in order to assess the impact of mono- versus trivalent binding modes. 
As the analyte, the spike protein and several of its subunits are tested as well as inactivated SARS-CoV-2 and pseudo viruses. While binding of the peptide to the full-length spike protein can be observed, the subunits RBD and S1 do not exhibit binding in the employed concentrations. 
Variations of the amino acid sequence of the recombinant full-length spike proteins furthermore influence binding behavior. The peptide was coupled to DNA nanostructures that form a geometric complement to the trimeric structure of the spike protein binding sites. 
An increase in binding strength for trimeric peptide presentation compared to single peptide presentation could be generally observed in ELISA and was quantified in switchSENSE measurements. Binding to inactivated wild type viruses could be shown as well as qualitatively different binding behavior of the Alpha and Beta variants compared to the wild type virus strain in pseudo virus models.
Y1  - 2022
U6  - https://doi.org/10.1038/s41598-022-16914-9
SN  - 2045-2322
VL  - 12
IS  - 1
PB  - Macmillan Publishers Limited, part of Springer Nature
CY  - London
ER  -