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Journal Article

Aqueous self-assembly of a protein-mimetic ampholytic block copolypeptide

MPS-Authors
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Sun,  Jing
Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121199

Cernoch,  Peter
Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121975

Völkel,  Antje
Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

/persons/resource/persons121815

Schlaad,  Helmut       
Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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2323473_supp.pdf
(Supplementary material), 3MB

Citation

Sun, J., Cernoch, P., Völkel, A., Wei, Y., Ruokolainen, J., & Schlaad, H. (2016). Aqueous self-assembly of a protein-mimetic ampholytic block copolypeptide. Macromolecules, 49(15), 5494-5501. doi:10.1021/acs.macromol.6b00817.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-1A14-F
Abstract
This report describes the aggregation behavior of an ABC-type ampholytic block copolypeptide, poly(ethylene oxide)-block-poly(l-lysine)-block-poly(l-glutamate), in aqueous media in dependence of pH. Polypeptide secondary structures and self-assemblies are investigated by circular dichroism (CD), Fourier transform infrared (FT-IR) and NMR spectroscopy, zeta potential measurements, analytical ultracentrifugation (AUC), dynamic/static light scattering (DLS/SLS), and cryogenic transmission electron microscopy (cryo-TEM). The polymer chains tend to form vesicles when the hydrophobic polypeptide helix is located at the chain end (acidic pH) and are existing as single chains when it is located in the center and flanked by the two hydrophilic segments (basic pH). Precipitation occurs in the intermediate pH range due to polyion complexation of the charged polypeptide segments.