Structural studies of "aggregation-prone" peptide-analogues of teleostean egg chorion ZPB proteins

Biopolymers. 2014 Nov;102(6):427-36. doi: 10.1002/bip.22563.

Abstract

Egg envelopes of vertebrates are composed of a family of proteins called zona pellucida (ZP) proteins, which are distinguished by the presence of a common structural polymerizing motif, known as ZP domain. Teleostean fish chorion is a fibrous structure, consisting of protein members of the ZPB/ZP1 and the ZPC/ZP3 families, which are incorporated as tandemly repeating heterodimers inside chorion fibers. Computational analysis of multiple ZPB/ZP1 proteins from several teleostean species, reveals two potential "aggregation-prone" sequence segments, forming a specific polymerization interface (AG interface). These two peptides were synthesized and results are presented in this work from transmission electron microscopy, Congo red staining, X-ray fiber diffraction and ATR FT-IR, which clearly display the ability of these peptides to self-aggregate, forming amyloid-like fibrils. This, most probably implies that the AG interface of ZPB/ZP1 proteins plays an important role for the formation of the repeating ZPB-ZPC heterodimers, which constitute teleostean chorion fibrils.

Keywords: amyloid fibrils; functional protective amyloids; peptide-analogues; teleostean fish chorion; vitelline envelope; zona pellucida proteins.

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry
  • Amyloid / ultrastructure
  • Animals
  • Consensus Sequence
  • Egg Proteins / chemistry*
  • Fish Proteins / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Ovum / chemistry*
  • Peptides / chemistry*
  • Protein Aggregates*
  • Protein Multimerization
  • Sequence Alignment
  • Spectroscopy, Fourier Transform Infrared
  • Structural Homology, Protein
  • X-Ray Diffraction
  • Zona Pellucida / chemistry

Substances

  • Amyloid
  • Egg Proteins
  • Fish Proteins
  • Peptides
  • Protein Aggregates
  • chorion proteins