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Intercellular Instructed-Assembly Mimics Protein Dynamics To Induce Cell Spheroids.

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Researchers developed enzyme-instructed self-assembling peptides that mimic fibronectin unfolding. This peptide assembly drives cell sheet transformation into spheroids, offering new control over cell behavior.

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Area of Science:

  • Biomaterials Science
  • Cell Biology
  • Biochemistry

Background:

  • Cell-mediated extracellular matrix (ECM) remodeling is crucial for cell functions.
  • Mimicking the dynamic nature of ECM proteins in synthetic materials remains a significant challenge.

Purpose of the Study:

  • To develop synthetic peptide assemblies that mimic protein dynamics in the ECM.
  • To demonstrate how these assemblies can control cell morphology and behavior, specifically cell spheroid formation.

Main Methods:

  • Enzyme-instructed self-assembly of phosphopeptides into nanoparticles and then nanofibers.
  • Utilizing phosphatases to catalyze peptide dephosphorylation in the intercellular space.
  • Investigating structure-activity relationships and interactions with ECM components.

Main Results:

  • Intercellular morphological transition of peptide assemblies successfully mimicked fibronectin unfolding.
  • Formation of cell spheroids from a monolayer of HS-5 cells was achieved via enzyme-instructed self-assembly.
  • Proteolytic stability, dephosphorylation, and biotin conjugation were identified as critical peptide features for spheroid formation.

Conclusions:

  • This study presents the first example of intercellular instructed-assembly from homotypic precursors.
  • The findings illustrate a novel approach using cell-responsive peptide assemblies to mimic protein dynamics and control cell behaviors.
  • The developed peptide assemblies interact with ECM components like laminin and collagens to drive cell spheroid formation.