surface plasmon resonance (spr) biacore analysis  (Biacore)

Journal: Biological Research

Article Title: Development of synthetic modulator enabling long-term propagation and neurogenesis of human embryonic stem cell-derived neural progenitor cells

doi: 10.1186/s40659-023-00471-0

Figure Lengend Snippet: Design and characterization of FGFR-agonist. ( A ) The secondary structures of the FGFR-binder and FGFR-agonist determined using Mfold software are presented, indicating the formation of a stem-loop structure. ( B ) The secondary structure of DNA-based FGFR-agonist is verified using native polyacrylamide gel electrophoresis (PAGE). This panel also includes the determined molecular weights of the single-stranded FGFR-binder, FGFR1-agonist, and a control oligonucleotide (Ctrl oligo). ( C ) SPR sensorgrams showing the real-time binding kinetics of FGFR-agonist aptamer to immobilized FGFR1 extracellular domain at various concentrations. The sensorgrams are color-coded based on the concentrations of the FGFR-binder (1, 2, 4, 8, 16 and 32 nM) and FGFR-agonist (0.16, 0.31, 0.625, 1.25, 2.5, 5 and 10 nM), respectively. ( D ) The relative binding performance of FGFR-binder and FGFR-agonist to the NIH3T3 cells was determined by flow cytometry (refer to Fig. for additional details)

Article Snippet: The sensorgrams are color-coded based on the concentrations of the FGFR-binder (1, 2, 4, 8, 16 and 32 nM) and FGFR-agonist (0.16, 0.31, 0.625, 1.25, 2.5, 5 and 10 nM), respectively. ( D ) The relative binding performance of FGFR-binder and FGFR-agonist to the NIH3T3 cells was determined by flow cytometry (refer to Fig. for additional details) To elucidate the molecular binding properties of the monomeric FGFR-binder and bivalent FGFR1-agonist with the extracellular domain of FGFR1, we employed Surface Plasmon Resonance (SPR) analysis using the Biacore method.

Techniques: Software, Polyacrylamide Gel Electrophoresis, Control, Binding Assay, Flow Cytometry