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

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.

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Sun, Jing1, Author              
Cernoch, Peter1, Author              
Völkel, Antje1, Author              
Wei, Yuhan, Author
Ruokolainen, Janne, Author
Schlaad, Helmut1, Author              
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1Kolloidchemie, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863288              

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 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.

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 Dates: 2016-07-192016
 Publication Status: Published in print
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 Identifiers: DOI: 10.1021/acs.macromol.6b00817
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Title: Macromolecules
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Chemical Society
Pages: - Volume / Issue: 49 (15) Sequence Number: - Start / End Page: 5494 - 5501 Identifier: ISSN: 0024-9297