TY - JOUR ID - 10442/17491 A1 - Louros N.N. A1 - A1 - Chrysina E.D. A1 - A1 - Baltatzis G.E. A1 - A1 - Patsouris E.S. A1 - A1 - Hamodrakas S.J. A1 - A1 - Iconomidou V.A. Y1 - 2016/// T1 - A common “aggregation-prone” interface possibly participates in the self-assembly of human zona pellucida proteins JF - FEBS Letters VL - 590 IS - 5 SN - 0014-5793 U3 - 10.1002/1873-3468.12099 PB - Wiley Blackwell SP - 619–630EP - UR - https://hdl.handle.net/10442/17491 N2 - 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. ER -