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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.
Verfasserangaben: | 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 |
Titel des übergeordneten Werks (Englisch): | Macromolecules : a publication of the American Chemical Society |
Verlag: | American Chemical Society |
Verlagsort: | Washington |
Publikationstyp: | Wissenschaftlicher Artikel |
Sprache: | Englisch |
Jahr der Erstveröffentlichung: | 2016 |
Erscheinungsjahr: | 2016 |
Datum der Freischaltung: | 22.03.2020 |
Band: | 49 |
Seitenanzahl: | 8 |
Erste Seite: | 5494 |
Letzte Seite: | 5501 |
Fördernde Institution: | Max Planck Society; Alexander von Humboldt Foundation; Natural Science Foundation of Shandong Province [ZR2015EM015]; Taishan Scholars Program |
Organisationseinheiten: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Chemie |
Peer Review: | Referiert |