N40, a novel nonacidic matrix protein from pearl oyster nacre, facilities nucleation of aragonite in vitro

Academic Article

Abstract

  • A novel nonacidic matrix protein from pearl oyster nacre has been purified by cation-exchange chromatography. It was designated N40 for the nacreous protein of approximately 40 kDa. On the basis of the extraction method (with Tris-buffered Milli-Q water) and amino acid compositions (Gly- and Ala-rich), N40 was inferred to be a conventional "insoluble matrix protein". Crystallization experiments showed that N40 could facilitate the nucleation of aragonite drastically. So far, among the macromolecules that have been purified from the shell, N40 is an exclusive protein that can nucleate aragonite by itself, without the need for adsorption to a substrate. Thus, the present study has proposed the possibility that the nonacidic shell protein (maybe a conventional "insoluble framework protein") can also directly participate in aragonite nucleation and even act as a nucleation site. It is a valuable supplement to the classic biomineralization theory, in which the soluble acidic proteins of the shell are generally believed to function as a nucleation site. © 2007 American Chemical Society.
  • Authors

    Published In

  • Biomacromolecules  Journal
  • Digital Object Identifier (doi)

    Author List

  • Yan Z; Jing G; Gong N; Li C; Zhou Y; Xie L; Zhang R
  • Start Page

  • 3597
  • End Page

  • 3601
  • Volume

  • 8
  • Issue

  • 11