Rational design based on multi-monomer simultaneous docking for epitope imprinting of SARS-CoV-2 spike protein.

Autor: Rajpal S; Institute of Analytical and Bioanalytical Chemistry (IABC), Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.; Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, New Delhi, 110016, India., Batista AD; Institute of Analytical and Bioanalytical Chemistry (IABC), Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.; Hahn-Schickard, Sedanstraße 14, 89077, Ulm, Germany., Groß R; Institute of Molecular Virology (IMV), Ulm University Medical Center, Meyerhofstraße 1, 89081, Ulm, Germany., Münch J; Institute of Molecular Virology (IMV), Ulm University Medical Center, Meyerhofstraße 1, 89081, Ulm, Germany., Mizaikoff B; Institute of Analytical and Bioanalytical Chemistry (IABC), Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany. boris.mizaikoff@uni-ulm.de.; Hahn-Schickard, Sedanstraße 14, 89077, Ulm, Germany. boris.mizaikoff@uni-ulm.de., Mishra P; Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology Delhi, New Delhi, 110016, India. pmishra@dbeb.iitd.ac.in.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 Oct 04; Vol. 14 (1), pp. 23057. Date of Electronic Publication: 2024 Oct 04.
DOI: 10.1038/s41598-024-73114-3
Abstrakt: Among biomimetic strategies shaping engineering designs, molecularly imprinted polymer (MIP) technology stands out, involving chemically synthesised receptors emulating natural antigen-antibody interactions. These versatile 'designer polymers' with remarkable stability and low cost, are pivotal for in vitro diagnostics. Amid the recent global health crisis, we probed MIPs' potential to capture SARS-CoV-2 virions. Large biotemplates complicate MIP design, influencing generated binding site specificity. To precisely structure recognition sites within polymers, we innovated an epitope imprinting method supplemented by in silico polymerization component screening. A viral surface Spike protein informed epitope selection was targeted for MIP development. A novel multi-monomer docking approach (MMSD) was employed to simulate classical receptor-ligand interactions, mimicking binding reinforcement across multiple amino acids. Around 40 monomer combinations were docked to the epitope sequence and top performers experimentally validated via rapid fluorescence binding assays. Notably, high imprinting factor polymers correlated with MMSD predictions, promising rational MIP design applicable to diverse viral pathologies.
(© 2024. The Author(s).)
Databáze: MEDLINE
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