Asprich mollusk shell protein: In vitro experiments aimed at elucidating function in CaCO3 crystallization

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Yael Politi - , Weizmann Institute of Science (Author)
  • Julia Mahamid - , Weizmann Institute of Science (Author)
  • Harvey Goldberg - , Western University (Author)
  • Steve Weiner - , Weizmann Institute of Science (Author)
  • Lia Addadi - , Weizmann Institute of Science (Author)

Abstract

Acidic proteins are key components of the organic matrix of many biologically formed minerals and are therefore thought to play an important role in their formation. Here we study the effect of one unusually acidic protein of the Asprich family, associated with mollusk shell prismatic layer, on the precipitation of CaCO3 in vitro. We show that Asprich induces and transiently stabilizes the deposition of amorphous calcium carbonate (ACC). Asprich also induces the formation of ACC when adsorbed onto chitin, a major component of the intracrystalline organic matrix of the prismatic layer. Based on this evidence, combined with previous studies on the forming prisms in the shell layer, we suggest that the in vivo function of Asprich is inducing and stabilizing ACC particles and inhibiting their uncontrolled crystallization until they undergo secondary nucleation on the growing prisms.

Details

Original languageEnglish
Pages (from-to)1171-1177
Number of pages7
JournalCrystEngComm
Volume9
Issue number12
Publication statusPublished - 2007
Peer-reviewedYes
Externally publishedYes

External IDs

ORCID /0000-0002-2872-8277/work/142239178