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

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

Author information

1
Department of Cell Biology and Biophysics, Faculty of Biology, University of Athens, Greece.
2
Institute of Biology, Medicinal Chemistry and Biotechnology, National Hellenic Research Foundation, Athens, Greece.
3
1st Department of Pathology, Medical School, University of Athens, Greece.

Abstract

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

PMID:
26879157
DOI:
10.1002/1873-3468.12099
[Indexed for MEDLINE]
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