Characterisation of aptamer-anchored poly(EDMA-co-GMA) monolith for high throughput affinity binding.

ABSTRACT: Immobilisation of aptameric ligands on solid stationary supports for effective binding of target molecules requires understanding of the relationship between aptamer-polymer interactions and the conditions governing the mass transfer of the binding process. Herein, key process parameters affecting the molecular anchoring of a thrombin-binding aptamer (TBA) onto polymethacrylate monolith pore surface, and the binding characteristics of the resulting macroporous aptasensor were investigated. Molecular dynamics (MD) simulations of the TBA-thrombin binding indicated enhanced Guanine 4 (G4) structural stability of TBA upon interaction with thrombin in an ionic environment. Fourier-transform infrared spectroscopy and thermogravimetric analyses were used to characterise the available functional g

SUBMITTER: Acquah C 

PROVIDER: S-EPMC6787036 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature