1 research outputs found
Recommended from our members
Glycosylated Peptoid Nanosheets as a Multivalent Scaffold for Protein Recognition
Glycoproteins adhered on the cellular
membrane play a pivotal role
in a wide range of cellular functions. Their importance is particularly
relevant in the recognition process between infectious pathogens (such
as viruses, bacteria, toxins) and their host cells. Multivalent interactions
at the pathogen-cell interfaces govern binding events and can result
in a strong and specific interaction. Here we report an approach to
mimic the cell surface presentation of carbohydrate ligands by the
multivalent display of sugars on the surface of peptoid nanosheets.
The constructs provide a highly organized 2D platform for recognition
of carbohydrate-binding proteins. The sugars were displayed using
different linker lengths or within loops containing 2–6 hydrophilic
peptoid monomers. Both the linkers and the loops contained one alkyne-bearing
monomer, to which different saccharides were attached by copper-catalyzed
azide–alkyne cycloaddition reactions. Peptoid nanosheets functionalized
with different saccharide groups were able to selectively bind multivalent
lectins, Concanavalin A and Wheat Germ Agglutinin, as observed by
fluorescence microscopy and a homogeneous Förster resonance
energy transfer (FRET)-based binding assay. To evaluate the potential
of this system as sensor for threat agents, the ability of functionalized
peptoid nanosheets to bind Shiga toxin was also studied. Peptoid nanosheets
were functionalized with globotriose, the natural ligand of Shiga
toxin, and the effective binding of the nanomaterial was verified
by the FRET-based binding assay. In all cases, evidence for multivalent
binding was observed by systematic variation of the ligand display
density on the nanosheet surface. These cell surface mimetic nanomaterials
may find utility in the inactivation of pathogens or as selective
molecular recognition elements