Calcified Tissue International

, Volume 72, Issue 5, pp 548–554 | Cite as

Chitin-Silk Fibroin Interactions: Relevance to Calcium Carbonate Formation in Invertebrates

  • G. FaliniEmail author
  • S. Weiner
  • L. Addadi


In mineralized tissues chitin is almost always associated with proteins, many of which are known to have chitin recognition consensus sequences. It has been observed in some mollusk shells that there is a well-defined spatial relation between the crystallographic axes of the crystals and the chitin fibrils. This implies that the chitin functions directly or indirectly as a template for nucleation of the mineral phase. It is thus of much interest to understand the exact nature of the interface between the chitin and the proteins at the molecular level in mineralized tissues. Chitin/silk fibroin interactions were studied in vitro at the molecular level using homogenous films composed of the two macromolecules. The results show that the silk fibroin intercalates between the molecular planes of the chitin, and that the interactions are mainly through the chitin acetyl groups. Published X-ray diffraction patterns and infrared spectra of mineralized tissue organic matrices, as well as infrared spectra reported here of the squid pen and lobster cuticle, all show that in vivo the chitin and protein are not intimately mixed, but exist as two phases. We deduce that there is an interfacial plane between them in which the interactions are through the amide groups.


Fibril Chitin Calcium Carbonate Infrared Spectrum Spatial Relation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  1. 1.Department of Structural BiologyWeizmann Institute of Science, 76100 RehovotIsrael
  2. 2.Dipartimento di Chimica “G. Ciamician”Alma Mater Studiorum Università di Bologna, via Selmi 2, 40126 BolognaItaly

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