Self-Assembly of α-Helical Polypeptides Driven by Complex Coacervation

Dimitrios Priftis, Lorraine Leon, Ziyuan Song, Sarah L. Perry, Khatcher O. Margossian, Anna Tropnikova, Jianjun Cheng, Matthew Tirrell

Research output: Contribution to journalArticlepeer-review

Abstract

Reported is the ability of α-helical polypeptides to self-assemble with oppositely-charged polypeptides to form liquid complexes while maintaining their α-helical secondary structure. Coupling the α-helical polypeptide to a neutral, hydrophilic polymer and subsequent complexation enables the formation of nanoscale coacervate-core micelles. While previous reports on polypeptide complexation demonstrated a critical dependence of the nature of the complex (liquid versus solid) on chirality, the α-helical structure of the positively charged polypeptide prevents the formation of β-sheets, which would otherwise drive the assembly into a solid state, thereby, enabling coacervate formation between two chiral components. The higher charge density of the assembly, a result of the folding of the α-helical polypeptide, provides enhanced resistance to salts known to inhibit polypeptide complexation. The unique combination of properties of these materials can enhance the known potential of fluid polypeptide complexes for delivery of biologically relevant molecules.

Original languageEnglish (US)
Pages (from-to)11128-11132
Number of pages5
JournalAngewandte Chemie - International Edition
Volume54
Issue number38
DOIs
StatePublished - Jan 1 2015

Keywords

  • chirality
  • helical structures
  • micelles
  • peptides
  • self-assembly

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)

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