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|Title:||Purification and characterization of a vaterite-inducing peptide, pelovaterin, from the eggshells of Pelodiscus sinensis (Chinese soft-shelled turtle)|
|Authors:||Lakshminarayanan, R. |
|Citation:||Lakshminarayanan, R., Chi-Jin, E.O., Loh, X.J., Kini, R.M., Valiyaveettil, S. (2005-05). Purification and characterization of a vaterite-inducing peptide, pelovaterin, from the eggshells of Pelodiscus sinensis (Chinese soft-shelled turtle). Biomacromolecules 6 (3) : 1429-1437. ScholarBank@NUS Repository. https://doi.org/10.1021/bm049276f|
|Abstract:||Proteins play a crucial role in the biomineralization of hard tissues such as eggshells. We report here the purification, characterization, and in vitro mineralization studies of a peptide, pelovaterin, extracted from eggshells of a soft-shelled turtle. It is a glycine-rich peptide with 42 amino acid residues and three disulfide bonds. When tested in vitro, the peptide induced the formation of a metastable vaterite phase. The floret-shaped morphology formed at a lower concentration (∼1 μM) was transformed into spherical particles at higher concentrations (>500 μM). The solution properties of the peptide are investigated by circular dichroism (CD), fluorescence emission spectroscopy, and dynamic light scattering (DLS) experiments. The conformation of pelovaterin changed from an unordered state at a low concentration to a β-sheet structure at high concentrations. Fluorescence emission studies indicated that the quantum yield is significantly decreased at higher concentrations, accompanied by a blue shift in the emission maximum. At higher concentrations a red-edge excitation shift was observed, indicating the restricted mobility of the peptide. On the basis of these observations, we discuss the presence of a peptide concentration-dependent monomer-multimer equilibrium in solution and its role in controlling the nucleation, growth, and morphology of CaCO3 crystals. This is the first peptide known to induce the nucleation and stabilization of the vaterite phase in solution. © 2005 American Chemical Society.|
|Appears in Collections:||Staff Publications|
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