Aqueous Self-Assembly of a Protein-Mimetic Ampholytic Block Copolypeptide

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

Tutkijat

Organisaatiot

  • Max Planck Institute of Colloids and Interfaces
  • Qingdao University of Science and Technology
  • University of Potsdam

Kuvaus

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.

Yksityiskohdat

AlkuperäiskieliEnglanti
Sivut5494-5501
Sivumäärä8
JulkaisuMacromolecules
Vuosikerta49
Numero15
TilaJulkaistu - 9 elokuuta 2016
OKM-julkaisutyyppiA1 Julkaistu artikkeli, soviteltu

ID: 6944657