Significance of the N- and C-terminal regions of CAP-1, a cuticle calcification-associated peptide from the exoskeleton of the crayfish, for calcification.

Abstract:

:Calcification-associated peptide (CAP)-1 is considered to play an important role in calcification of the exoskeleton of the crayfish, Procambarus clarkii. In this study, in order to clarify the molecular mechanism of calcification, we constructed expression systems of recombinant molecules of CAP-1 and its related peptides in Escherichia coli, and verified the structure-activity relationship of these peptides. The inhibitory assay on calcium carbonate precipitation and the calcium-binding assay showed that the C-terminal acidic region was most important for both activities. The CD spectra of these peptides varied depending on calcium concentration and showed that the N-terminal region is associated with the peptide conformation. These results indicate that the C-terminal part of CAP-1 may concentrate calcium ions for nucleation and/or interact with calcium carbonate precipitate to control the growth and that the N-terminal part contribute to maintaining the peptide conformation.

journal_name

Peptides

journal_title

Peptides

authors

Inoue H,Ohira T,Nagasawa H

doi

10.1016/j.peptides.2006.12.005

subject

Has Abstract

pub_date

2007-03-01 00:00:00

pages

566-73

issue

3

eissn

0196-9781

issn

1873-5169

pii

S0196-9781(06)00574-2

journal_volume

28

pub_type

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