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Surface functionalization with short PAS-sequence affects H-ferritin nanocage stability.

Ilaria Tagliolini1, Francesca Gorgoglione1, Marta Sevieri1

  • 1Dipartimento di Scienze Biomediche e Cliniche, Università degli studi di Milano, 20157, Milano, Italy.

International Journal of Biological Macromolecules
|September 21, 2025
PubMed
Summary

PASylation with shorter domains, like 20 amino acids, destabilizes H-ferritin nanocages (HFn). This impacts HFn stability and assembly, crucial for their tumor-targeting delivery applications.

Keywords:
H-ferritin nanocagesNanodrug delivery systemPASylation

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Area of Science:

  • Biochemistry
  • Nanotechnology
  • Structural Biology

Background:

  • H-ferritin nanocages (HFn) are effective tumor-targeting delivery systems.
  • Clinical use is limited by HFn's short half-life and rapid clearance.
  • PASylation extends HFn half-life, but the impact of shorter PAS domains is unknown.

Purpose of the Study:

  • Investigate the effect of shorter PAS domains on HFn stability.
  • Analyze the structural dynamics of HFn modified with 20 amino acid PAS domains (PAS20-HFn).

Main Methods:

  • Production and purification of PAS20-HFn monomers.
  • Structural dynamics simulations of native HFn, PAS20-HFn, and PAS40-HFn complexes (dimers, tetramers, octamers).

Main Results:

  • PAS20-HFn monomers were produced but failed to form stable quaternary structures.
  • Simulations revealed increased flexibility in PAS20-HFn tetramers within specific helical regions.
  • PASylation disrupted proper C-terminal helix association in PAS20-HFn octamers, causing nanocage instability.

Conclusions:

  • Shorter PAS domains (20 amino acids) negatively impact HFn stability and assembly.
  • PASylation length is critical for maintaining HFn nanocage integrity and function.
  • Findings highlight the importance of PAS domain length for HFn-based delivery systems.