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Mimicking the Function of Eggshell Matrix Proteins: The Role of Multiplets of Charged Amino Acid Residues and Self‐Assembly of Peptides in Biomineralization
Author(s) -
Ajikumar Parayil Kumaran,
Vivekanandan Subramanian,
Lakshminarayanan Rajamani,
Jois Seetharama D. S.,
Kini R. Manjunatha,
Valiyaveettil Suresh
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200500261
Subject(s) - biomineralization , eggshell , crystallite , chemistry , calcite , matrix (chemical analysis) , peptide , crystallography , nucleation , eggshell membrane , biophysics , chemical engineering , mineralogy , biochemistry , organic chemistry , biology , chromatography , membrane , engineering , ecology
An eggshell finish : Designed peptides can be used as a tool to unravel the structure–activity relationships of eggshell matrix proteins. The ordered arrangement of doublets of charged residues on the peptide and its self‐assembling characteristics play a key role in the biomimetic nucleation of polycrystalline calcite crystal aggregates (see picture), which models that initiated by the goose eggshell matrix protein, ansocalcin.