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Title: Using Biomimetic Polymers in Place of Noncollagenous Proteins to Achieve Functional Remineralization of Dentin Tissues

Abstract

In calcified tissues such as bones and teeth, mineralization is regulated by an extracellular matrix, which includes non-collagenous proteins (NCP). This natural process has been adapted or mimicked to restore tissues following physical damage or demineralization by using polyanionic acids in place of NCPs, but the remineralized tissues fail to fully recover their mechanical properties. Here we show that pre-treatment with certain amphiphilic peptoids, a class of peptide-like polymers consisting of N-substituted glycines that have defined monomer sequences, enhances ordering and mineralization of collagen and induces functional remineralization of dentin lesions in vitro. In the vicinity of dentin tubules, the newly formed apatite nano-crystals are co-aligned with the c-axis parallel to the tubular periphery and recovery of tissue ultrastructure is accompanied by development of high mechanical strength. The observed effects are highly sequence-dependent with alternating polar and non-polar groups leading to positive outcomes while diblock sequences have no effect. The observations suggest aromatic groups interact with the collagen while the hydrophilic side chains bind the mineralizing constituents and highlight the potential of synthetic sequence-defined biomimetic polymers to serve as NCP mimics in tissue remineralization.

Authors:
ORCiD logo [1];  [2];  [3];  [3];  [4];  [2]; ORCiD logo [4];  [3];  [3]; ORCiD logo [5]
  1. Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States; Department of Preventive and Restorative Dental Sciences, University of California, San Francisco, California 94143, United States
  2. Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, United States
  3. Department of Preventive and Restorative Dental Sciences, University of California, San Francisco, California 94143, United States
  4. Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States
  5. Molecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States; Physical Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99352, United States; Department of Materials Science and Engineering, University of Washington, Seattle, Washington 98195, United States
Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1422314
Report Number(s):
PNNL-SA-125917
Journal ID: ISSN 2373-9878
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Journal Name:
ACS Biomaterials Science & Engineering
Additional Journal Information:
Journal Volume: 3; Journal Issue: 12; Journal ID: ISSN 2373-9878
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English

Citation Formats

Chien, Yung-Ching, Tao, Jinhui, Saeki, Kuniko, Chin, Alexander F., Lau, Jolene L., Chen, Chun-Long, Zuckermann, Ronald N., Marshall, Sally J., Marshall, Grayson W., and De Yoreo, James J. Using Biomimetic Polymers in Place of Noncollagenous Proteins to Achieve Functional Remineralization of Dentin Tissues. United States: N. p., 2017. Web. doi:10.1021/acsbiomaterials.7b00378.
Chien, Yung-Ching, Tao, Jinhui, Saeki, Kuniko, Chin, Alexander F., Lau, Jolene L., Chen, Chun-Long, Zuckermann, Ronald N., Marshall, Sally J., Marshall, Grayson W., & De Yoreo, James J. Using Biomimetic Polymers in Place of Noncollagenous Proteins to Achieve Functional Remineralization of Dentin Tissues. United States. doi:10.1021/acsbiomaterials.7b00378.
Chien, Yung-Ching, Tao, Jinhui, Saeki, Kuniko, Chin, Alexander F., Lau, Jolene L., Chen, Chun-Long, Zuckermann, Ronald N., Marshall, Sally J., Marshall, Grayson W., and De Yoreo, James J. Thu . "Using Biomimetic Polymers in Place of Noncollagenous Proteins to Achieve Functional Remineralization of Dentin Tissues". United States. doi:10.1021/acsbiomaterials.7b00378.
@article{osti_1422314,
title = {Using Biomimetic Polymers in Place of Noncollagenous Proteins to Achieve Functional Remineralization of Dentin Tissues},
author = {Chien, Yung-Ching and Tao, Jinhui and Saeki, Kuniko and Chin, Alexander F. and Lau, Jolene L. and Chen, Chun-Long and Zuckermann, Ronald N. and Marshall, Sally J. and Marshall, Grayson W. and De Yoreo, James J.},
abstractNote = {In calcified tissues such as bones and teeth, mineralization is regulated by an extracellular matrix, which includes non-collagenous proteins (NCP). This natural process has been adapted or mimicked to restore tissues following physical damage or demineralization by using polyanionic acids in place of NCPs, but the remineralized tissues fail to fully recover their mechanical properties. Here we show that pre-treatment with certain amphiphilic peptoids, a class of peptide-like polymers consisting of N-substituted glycines that have defined monomer sequences, enhances ordering and mineralization of collagen and induces functional remineralization of dentin lesions in vitro. In the vicinity of dentin tubules, the newly formed apatite nano-crystals are co-aligned with the c-axis parallel to the tubular periphery and recovery of tissue ultrastructure is accompanied by development of high mechanical strength. The observed effects are highly sequence-dependent with alternating polar and non-polar groups leading to positive outcomes while diblock sequences have no effect. The observations suggest aromatic groups interact with the collagen while the hydrophilic side chains bind the mineralizing constituents and highlight the potential of synthetic sequence-defined biomimetic polymers to serve as NCP mimics in tissue remineralization.},
doi = {10.1021/acsbiomaterials.7b00378},
journal = {ACS Biomaterials Science & Engineering},
issn = {2373-9878},
number = 12,
volume = 3,
place = {United States},
year = {2017},
month = {11}
}

Works referencing / citing this record:

The Self-Assembling Peptide P 11 -4 Prevents Collagen Proteolysis in Dentin
journal, November 2018

  • de Sousa, J. P.; Carvalho, R. G.; Barbosa-Martins, L. F.
  • Journal of Dental Research, Vol. 98, Issue 3
  • DOI: 10.1177/0022034518817351