TY  - JOUR
A1  - Bognár, Zsófia
A1  - Supala, Eszter
A1  - Yarman, Aysu
A1  - Zhang, Xiaorong
A1  - Bier, Frank Fabian
A1  - Scheller, Frieder W.
A1  - Gyurcsanyi, Róbert E.
T1  - Peptide epitope-imprinted polymer microarrays for selective protein recognition
BT  - application for SARS-CoV-2 RBD protein
JF  - Chemical science / RSC, Royal Society of Chemistry
N2  - We introduce a practically generic approach for the generation of epitope-imprinted polymer-based microarrays for protein recognition on surface plasmon resonance imaging (SPRi) chips. The SPRi platform allows the subsequent rapid screening of target binding kinetics in a multiplexed and label-free manner. The versatility of such microarrays, both as synthetic and screening platform, is demonstrated through developing highly affine molecularly imprinted polymers (MIPs) for the recognition of the receptor binding domain (RBD) of SARS-CoV-2 spike protein. A characteristic nonapeptide GFNCYFPLQ from the RBD and other control peptides were microspotted onto gold SPRi chips followed by the electrosynthesis of a polyscopoletin nanofilm to generate in one step MIP arrays. A single chip screening of essential synthesis parameters, including the surface density of the template peptide and its sequence led to MIPs with dissociation constants (K-D) in the lower nanomolar range for RBD, which exceeds the affinity of RBD for its natural target, angiotensin-convertase 2 enzyme. Remarkably, the same MIPs bound SARS-CoV-2 virus like particles with even higher affinity along with excellent discrimination of influenza A (H3N2) virus. While MIPs prepared with a truncated heptapeptide template GFNCYFP showed only a slightly decreased affinity for RBD, a single mismatch in the amino acid sequence of the template, i.e. the substitution of the central cysteine with a serine, fully suppressed the RBD binding.
Y1  - 2021
U6  - https://doi.org/10.1039/d1sc04502d
SN  - 2041-6539
VL  - 13
IS  - 5
SP  - 1263
EP  - 1269
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  -