Tuning the Dynamics of Viral-Factories-Inspired Compartments Formed by Peptide–RNA Liquid–Liquid Phase Separation

Itai Katzir, Elvira Haimov, Ayala Lampel*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Viral factories are intracellular microcompartments formed by mammalian viruses in their host cells, and contain necessary machinery for viral genome replication, capsid assembly, and maturation, thus serving as “factories” for formation of new viral particles. Recent evidence suggests that these compartments are formed by liquid–liquid phase separation (LLPS) of viral proteins and nucleic acids and present dynamic properties. In this work, inspired by the remarkable functionalities of viral factories, dynamic compartments that are formed by complexation between a minimalistic, disordered peptide and RNA are designed. By systematic studies using sequence variants it is shown that the material properties of the compartments can be modulated by changes to the peptide sequence, at the single amino acid level. Moreover, by taking this approach to the next step, liquid compartments with light-induced tunable dynamics are developed. The results demonstrate that the material properties of liquid droplets can be temporally regulated by increasing peptide polarity and charge, and that these changes can be further utilized for controlled partitioning and release of payloads from the compartments.

Original languageEnglish
Article number2206371
JournalAdvanced Materials
Volume34
Issue number47
DOIs
StatePublished - 24 Nov 2022

Keywords

  • coacervates
  • liquid droplets
  • liquid–liquid phase separation
  • membraneless organelles
  • peptides
  • viral factories

Fingerprint

Dive into the research topics of 'Tuning the Dynamics of Viral-Factories-Inspired Compartments Formed by Peptide–RNA Liquid–Liquid Phase Separation'. Together they form a unique fingerprint.

Cite this