Chemoenzymatic oligomerisation of l-amino acids was successfully developed using mechanochemical techniques.

The structure and characterization of the oligopeptide crystals formed from the feather keratin solution obtained by superheated water treatment are reported. The FTIR spectra and 1H and 13C solid‐state NMR results indicate that the peptides, arranged mostly in a beta‐sheet structure in feather, reorganize into a mainly alpha‐helix and less beta‐sheet mixed secondary structure, when self‐assemble from the solution at room temperature. MALDI‐ToF‐ToF spectra confirm that the most primary sequence with the mass 1884 come from the feather keratin 4, KRFA_CHICK of Gallus gallus. The largely preservation of all but cystine amino acid species and the increase of hydrophobic amino acids content in the oligopeptide crystals are proved by the amino acid analysis.

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