A synthesis approach to understanding repeated peptides conserved in mineralization proteins.

A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Research Abstract Details 

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A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Abstract Text:

Kiyotaka Shiba,Tamiko Minamisawa,

We created artificial proteins that contained repeats of a short peptide motif, Asn-Gly-Asx. In nature this motif is repeated within shell proteins as an idiosyncratic domain, while in vitro it has been shown to suppress calcification. The motif was embedded within peptide sequences that did or did not have the ability to form secondary structures, which provided the motif with a variety of physicochemical properties. Although a short synthetic peptide containing the motif did not inhibit calcification in vitro, some of the artificial proteins carrying repeats of the motif did show robust suppression of calcification. Artificial proteins lacking the motif did not exhibit suppressive activity. Likewise, one construct containing multiple repeats of the motifs also did not exert an inhibitory effect on calcification. Apparently, carrying the Asn-Gly-Asx motif is not, by itself, sufficient for expression of its cryptic activity; instead, certain physicochemical properties of the polypeptides mediate its manifestation. We anticipate that syntheses using "motif programming", such as the one described here, will shed light on the origin of repetitive sequences as well as on the evolution of biomineralization proteins.

A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Publishing Authors By Initials

K Shiba,T Minamisawa,

For similar proteins research abstracts see: proteins research

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A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Biomacromolecules

VOLUME: 8

Page Numbers: 2659-64

Journal Abbreviation: Biomacromolecules

ISSN: 1525-7797

DAY: 1

MONTH: 08

YEAR: 2007

A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Information

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LANGUAGE: eng

NlmUniqueID: 100892849

A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Keywords Mesh Terms:

KEYWORDS: Proteins

MESH TERMS: chemistry

Chemical & Substance for Abstract: A synthesis approach to understanding repeated peptides conserved in mineralization proteins. Information

Substance Name: Calcium Carbonate

Registry Number: 471-34-1

Grant and Affiliation Information for A synthesis approach to understanding repeated peptides conserved in mineralization proteins.

AFFILIATION: Department of Protein Engineering, Cancer Institute, Japanese Foundation for Cancer Research, and Core Research for Evolutional Science and Technology, Japan Science and Technology Agency, Koto-ku, Tokyo 135-8550, Japan. kshiba@ jfcr.or.jp

Country: United States

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MEDLINETA: Biomacromolecules

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