Hyunji Park

Self-Assembly Process of Soft Ferritin-PNIPAAm Conjugate Bionanoparticles at Polar–Apolar Interfaces

We describe an in-depth investigation on the dynamics and assembly behavior at polar-apolar interfaces of ferritin-PNIPAAm conjugates (poly-N-isopropylacrylamide). The stabilization of oil-water interfaces by the modified ferritin was investigated by dynamic surface tension measurements and compared to the individual components of the bionanoparticle conjugate, namely, unmodified ferritin and pure PNIMAAm of similar molecular weight. It was found that the modified ferritin, even at a low particle concentration, rapidly reduces the interfacial tension. The difference in interfacial stabilization was also shown by cryo-scanning electron microscopy and scanning force microscopy, which displayed very different morphologies at the polar-apolar interface for the unmodified ferritin, pure PNIPAAm, and the ferritin-PNIPAAm conjugate, respectively. The self-assembly of the ferritin-PNIPAAm was further analyzed by cryo-transmission electron microscopy and fluorescence microscopy, for which a fluorescently labeled polymer was used. Both techniques revealed details on the assembly of the protein-polymer conjugate at the oil-water interface.

Glycopolymer Brushes for Specific Lectin Binding by Controlled Multivalent Presentation of N‐Acetyllactosamine Glycan Oligomers

A new multivalent glycopolymer platform for lectin recognition is introduced in this work by combining the controlled growth of glycopolymer brushes with highly specific glycosylation reactions. Glycopolymer brushes, synthetic polymers with pendant saccharides, are prepared by surface-initiated atom transfer radical polymerization (SI-ATRP) of 2-O-(N-acetyl-β-d-glucosamine)ethyl methacrylate (GlcNAcEMA). Here, the fabrication of multivalent glycopolymers consisting of poly(GlcNAcEMA) is reported with additional biocatalytic elongation of the glycans directly on the silicon substrate by specific glycosylation using recombinant glycosyltransferases. The bioactivity of the surface-grafted glycans is investigated by fluorescence-linked lectin assay. Due to the multivalency of glycan ligands, the glycopolymer brushes show very selective, specific, and strong interactions with lectins. The multiarrays of the glycopolymer brushes have a large potential as a screening device to define optimal-binding environments of specific lectins or as new simplified diagnostic tools for the detection of cancer-related lectins in blood serum.

Micelles from self-assembled double-hydrophilic PHEMA-glycopolymer-diblock copolymers as multivalent scaffolds for lectin binding

We introduce a novel double-hydrophilic hydroxyethylmethacrylate (HEMA) based diblock glycopolymer which self-assembles into homogeneous spherical micellar structures in water. The micellar structure renders surface-oriented N-acetylglucocosamine (GlcNAc) sugar moieties for strong multivalent glycan-mediated lectin binding. Structural analysis and lectin binding is performed by microscopy methods, dynamic light scattering (DLS) and two-focus fluorescence correlation spectroscopy (2fFCS), revealing a novel micellar type of multivalent sugar binding scaffold with high potential for biomedical applications.