| Autor: |
Skoulas D; Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany., Ojo OM; Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany., Thalhammer A; Institute of Biochemistry and Biology, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany., Kochovski Z; Institute for Electrochemical Energy Storage, Helmholtz-Zentrum Berlin, Hahn-Meitner Platz 1, 14109 Berlin, Germany., Schlaad H; Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany. |
| Abstrakt: |
A small series of copoly(α,l-glutamic acid/dl-allylglycine)s with the same chain length and allylglycine content (∼10 mol %) but different spatial distribution of allylglycine units was synthesized and subsequently glycosylated via thiol-ene chemistry. Dilute aqueous copolypeptide solutions (0.1 wt %, physiological saline) were analyzed by circular dichroism spectroscopy, dynamic light scattering, and cryogenic transmission electron microscopy. The copolypeptides adopted a random coil or α-helix conformation, depending on solution pH, and the glycosylated residues either distorted or enhanced the folding into an α-helix depending on their location and spatial distribution along the chain. However, regardless of their secondary structure and degree of charging, all partially glycosylated copolypeptides self-assembled into 3D spherical structures, supposedly driven by a hydrophilic effect promoting microphase separation into glucose-rich and glutamate-rich domains. |
