Aqueous Self-Assembly of a Protein-Mimetic Ampholytic Block Copolypeptide
- 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 (cryoTEM). 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.
Author details: | Jing Sun, Peter Cernoch, Antje Völkel, Yuhan Wei, Janne Ruokolainen, Helmut SchlaadORCiDGND |
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DOI: | https://doi.org/10.1021/acs.macromol.6b00817 |
ISSN: | 0024-9297 |
ISSN: | 1520-5835 |
Title of parent work (English): | Macromolecules : a publication of the American Chemical Society |
Publisher: | American Chemical Society |
Place of publishing: | Washington |
Publication type: | Article |
Language: | English |
Year of first publication: | 2016 |
Publication year: | 2016 |
Release date: | 2020/03/22 |
Volume: | 49 |
Number of pages: | 8 |
First page: | 5494 |
Last Page: | 5501 |
Funding institution: | Max Planck Society; Alexander von Humboldt Foundation; Natural Science Foundation of Shandong Province [ZR2015EM015]; Taishan Scholars Program |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie |
Peer review: | Referiert |