A Synthesis Approach to Understanding Repeated Peptides Conserved in Mineralization Proteins
- 1 August 2007
- journal article
- Published by American Chemical Society (ACS) in Biomacromolecules
- Vol. 8 (9), 2659-2664
- https://doi.org/10.1021/bm700652b
Abstract
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.Keywords
This publication has 36 references indexed in Scilit:
- Structure and expression of an unusually acidic matrix protein of pearl oyster shellsBiochemical and Biophysical Research Communications, 2004
- Control of Crystal Size and Lattice Formation by Starmaker in Otolith BiomineralizationScience, 2003
- The Complete Primary Structure of Molluscan Shell Protein 1 (MSP-1), an Acidic Glycoprotein in the Shell Matrix of the Scallop Patinopecten yessoensisMarine Biotechnology, 2001
- Protein Repeats: Structures, Functions, and EvolutionJournal of Structural Biology, 2001
- A census of protein repeatsJournal of Molecular Biology, 1999
- Cloning and sequencing of a gene encoding a new member of the tetratricopeptide protein family from magnetosomes of Magnetospirillum magnetotacticumGene, 1996
- The corrected structure of the SM50 spicule matrix protein of Strongylocentrotus purpuratusDevelopmental Biology, 1991
- Repeats of base oligomers as the primordial coding sequences of the primeval earth and their vestiges in modern genesJournal of Molecular Evolution, 1984
- Control of Calcium Carbonate Nucleation and Crystal Growth by Soluble Matrx of Oyster ShellScience, 1981
- Soluble Protein of the Organic Matrix of Mollusk Shells: A Potential Template for Shell FormationScience, 1975