Phosphorylated amelogenin N-terminal peptides regulate calcite crystal cluster formation in a water–acetonitrile system-Reference-Cited by-同舟云学术

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Phosphorylated amelogenin N-terminal peptides regulate calcite crystal cluster formation in a water–acetonitrile system

Published:2023 Issue:36 Volume:25 Page:5150-5159
ISSN:1466-8033
Container-title:CrystEngComm
language:en
Short-container-title:CrystEngComm

Author:

Zou Wenwu¹²,Lin Yutao¹²,Xie Zhenze¹²,Lin Yingxin¹²,Du Chang¹²³^ORCID

Affiliation:

1. School of Materials Science and Engineering, South China University of Technology, Guangzhou, 510641, China

2. National Engineering Research Center for Tissue Restoration and Reconstruction, Guangzhou, 510006, China

3. Key Laboratory of Biomedical Materials and Engineering of the Ministry of Education, South China University of Technology, Guangzhou 510006, China

Abstract

The function of phosphorylated organic additives can be enhanced by changing the secondary structure of the organic matrix which may provide a new strategy for novel crystal synthesis.

Funder

National Key Research and Development Program of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Condensed Matter Physics,General Materials Science,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/CE/D3CE00165B

Reference41 articles.

1. Protein- and Peptide-Directed Syntheses of Inorganic Materials

2. Biomimetic Model Systems for Investigating the Amorphous Precursor Pathway and Its Role in Biomineralization

3. Intrinsically disordered proteins and biomineralization

4. Intrinsically disordered -subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure

5. Protein-mediated Enamel Mineralization

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