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

Research output: Contribution to journalArticleScientificpeer-review

Researchers

Research units

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

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.

Details

Original languageEnglish
Pages (from-to)5494-5501
Number of pages8
JournalMacromolecules
Volume49
Issue number15
Publication statusPublished - 9 Aug 2016
MoE publication typeA1 Journal article-refereed

ID: 6944657