Mimicking the function of eggshell matrix proteins: The role of multiplets of charged amino acid residues and self-assembly of peptides in biomineralization

被引：22

作者：

Ajikumar, PK

Vivekanandan, S

Lakshminarayanan, R

Jois, SDS

Kini, RM

Valiyaveettil, S

机构：

[1] Natl Univ Singapore, Dept Chem, Singapore 117543, Singapore

[2] Natl Univ Singapore, Singapore MIT Alliance, Singapore 117543, Singapore

[3] Natl Univ Singapore, Dept Pharm, Singapore 117543, Singapore

[4] Natl Univ Singapore, Dept Biol Sci, Singapore 117543, Singapore

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2005年 / 44卷 / 34期

关键词：

biomineralization; eggshell; peptides; proteins; structure-activity relationships;

D O I：

10.1002/anie.200500261

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Figure Presented) 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. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：5476 / 5479

页数：4

共 57 条

[1] CONTROL AND DESIGN PRINCIPLES IN BIOLOGICAL MINERALIZATION [J].