A common 'aggregation‐prone' interface possibly participates in the self‐assembly of human zona pellucida proteins. Issue 5 (26th February 2016)

• Record Type: Journal Article
• Authors: Louros, Nikolaos N.; Chrysina, Evangelia D.; Baltatzis, Georgios E.; Patsouris, Efstratios S.; Hamodrakas, Stavros J.; Iconomidou, Vassiliki A.
• Is Part Of: FEBS letters. Volume 590:Issue 5(2016)
• Page Start: 619
• Page End: 630
• Publication Date: 2016-02-26
• Subjects: amyloid fibrils -- electron microscopy -- functional amyloid -- homology modeling -- peptide‐analogs -- zona pellucida; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12099
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract :