A common 'aggregation-prone' interface possibly participates in the self-assembly of human zona pellucida proteins

FEBS Lett. 2016 Mar;590(5):619-30. doi: 10.1002/1873-3468.12099. Epub 2016 Feb 26.


Human zona pellucida (ZP) is composed of four glycoproteins, namely ZP1, ZP2, ZP3 and ZP4. ZP proteins form heterodimers, which are incorporated into filaments through a common bipartite polymerizing component, designated as the ZP domain. The latter is composed of two individually folded subdomains, named ZP-N and ZP-C. Here, we have synthesized six 'aggregation-prone' peptides, corresponding to a common interface of human ZP2, ZP3 and ZP4. Experimental results utilizing electron microscopy, X-ray diffraction, ATR FT-IR spectroscopy and polarizing microscopy indicate that these peptides self-assemble forming fibrils with distinct amyloid-like features. Finally, by performing detailed modeling and docking, we attempt to shed some light in the self-assembly mechanism of human ZP proteins.

Keywords: amyloid fibrils; electron microscopy; functional amyloid; homology modeling; peptide-analogs; zona pellucida.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glycoproteins / chemistry*
  • Humans
  • Molecular Docking Simulation
  • Protein Aggregates*
  • Protein Multimerization
  • Protein Structure, Quaternary


  • Glycoproteins
  • Protein Aggregates