Abstract
AbstractIn situ monitoring of biomolecular recognition, especially at surfaces, still presents a significant technical challenge. Electron paramagnetic resonance (EPR) of biomolecules spin‐labeled with nitroxides can offer uniquely sensitive and selective insights into these processes, but new spin‐labeling strategies are needed. The synthesis and study of a bromoacrylaldehyde spin label (BASL), which features two attachment points with orthogonal reactivity is reported. The first examples of mannose and biotin ligands coupled to aqueous carboxy‐functionalized gold nanoparticles through a spin label are presented. EPR spectra were obtained for the spin‐labeled ligands both free in solution and attached to nanoparticles. The labels were recognized by the mannose‐binding lectin, Con A, and the biotin‐binding protein avidin‐peroxidase. Binding gave quantifiable changes in the EPR spectra from which binding profiles could be obtained that reflect the strength of binding in each case.
Highlights
The development of selective and non-perturbing molecular probes is vital for understanding the complex interactions of biological systems with biomolecules on surfaces
The labels were recognized by the mannosebinding lectin, concanavalin A (Con A), and the biotin-binding protein avidinperoxidase
The tetravalent mannose binding lectin concanavalin A (Con A), has an affinity for clustered membrane bound mannose moiety lipids 3-fold weaker than it has in solution.[9]
Summary
The development of selective and non-perturbing molecular probes is vital for understanding the complex interactions of biological systems with biomolecules on surfaces. The first examples of mannose and biotin ligands coupled to aqueous carboxy-functionalized gold nanoparticles through a spin label are presented. EPR spectra were obtained for the spin-labeled ligands both free in solution and attached to nanoparticles.
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