Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides

Model peptides were designed, synthesized and conducted a detailed structure-property study to unravel the molecular mechanism of goose eggshell calcification. The peptides were designed based on the primary structural features of the eggshell matrix proteins ansocalcin and OC-17. In vitro CaCO₃ cry...

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Main Authors: Ajikumar, Parayil Kumaran, Lakshminarayanan, Rajamani, Valiyaveettil, Suresh, Kini, R. Manjunatha
Format: Article
Language:en_US
Published: 2003
Subjects:
Online Access:http://hdl.handle.net/1721.1/3929
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author Ajikumar, Parayil Kumaran
Lakshminarayanan, Rajamani
Valiyaveettil, Suresh
Kini, R. Manjunatha
author_facet Ajikumar, Parayil Kumaran
Lakshminarayanan, Rajamani
Valiyaveettil, Suresh
Kini, R. Manjunatha
author_sort Ajikumar, Parayil Kumaran
collection MIT
description Model peptides were designed, synthesized and conducted a detailed structure-property study to unravel the molecular mechanism of goose eggshell calcification. The peptides were designed based on the primary structural features of the eggshell matrix proteins ansocalcin and OC-17. In vitro CaCO₃ crystal growth experiments in presence of these peptides showed calcite crystal aggregation as observed in the case of the parent protein ansocalcin. The structure of these peptides in solution was established using intrinsic tryptophan fluorescence studies and quasi-elastic light scattering experiments. The structural features are correlated with observed results of the in vitro crystallization studies.
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spelling mit-1721.1/39292019-04-10T18:40:00Z Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides Ajikumar, Parayil Kumaran Lakshminarayanan, Rajamani Valiyaveettil, Suresh Kini, R. Manjunatha ansocalcin biomineralization calcium carbonate designed peptides Model peptides were designed, synthesized and conducted a detailed structure-property study to unravel the molecular mechanism of goose eggshell calcification. The peptides were designed based on the primary structural features of the eggshell matrix proteins ansocalcin and OC-17. In vitro CaCO₃ crystal growth experiments in presence of these peptides showed calcite crystal aggregation as observed in the case of the parent protein ansocalcin. The structure of these peptides in solution was established using intrinsic tryptophan fluorescence studies and quasi-elastic light scattering experiments. The structural features are correlated with observed results of the in vitro crystallization studies. Singapore-MIT Alliance (SMA) 2003-12-16T02:43:43Z 2003-12-16T02:43:43Z 2004-01 Article http://hdl.handle.net/1721.1/3929 en_US Molecular Engineering of Biological and Chemical Systems (MEBCS); 262859 bytes application/pdf application/pdf
spellingShingle ansocalcin
biomineralization
calcium carbonate
designed peptides
Ajikumar, Parayil Kumaran
Lakshminarayanan, Rajamani
Valiyaveettil, Suresh
Kini, R. Manjunatha
Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides
title Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides
title_full Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides
title_fullStr Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides
title_full_unstemmed Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides
title_short Eggshell Matrix Protein Mimetics: Elucidation of Molecular Mechanism of Goose Eggshell Calcification using Designed Peptides
title_sort eggshell matrix protein mimetics elucidation of molecular mechanism of goose eggshell calcification using designed peptides
topic ansocalcin
biomineralization
calcium carbonate
designed peptides
url http://hdl.handle.net/1721.1/3929
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