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Title: Thermoreversible and Injectable ABC Polypeptoid Hydrogels: Controlling the Hydrogel Properties through Molecular Design

Abstract

Here, a series of ABC triblock copolypeptoids [i.e., poly(N-allyl glycine)-b-poly(N-methyl glycine)-b-poly(N-decyl glycine) (AMD)] with well-defined structure and varying composition have been synthesized by sequential primary amine-initiated ring-opening polymerization of the corresponding N-substituted N-carboxyanhydride monomers (Al-NCA, Me-NCA, and De-NCA). The ABC block copolypeptoids undergo sol-to-gel transitions with increasing temperature in water and biological media at low concentrations (2.5–10 wt %). The sol–gel transition is rapid and fully reversible with a narrow transition window, evidenced by the rheological measurements. The gelation temperature (Tgel) and mechanical stiffness of the hydrogels are highly tunable: Tgel in the 26.2–60.0 °C range, the storage modulus (G') and Young’s modulus (E) in the 0.2–780 Pa and 0.5–2346 Pa range, respectively, at the physiological temperature (37 °C) can be readily accessed by controlling the block copolypeptoid composition and the polymer solution concentration. The hydrogel is injectable through a 24 gauge syringe needle and maintains their shape upon in contact with surfaces or water baths that are kept above the sol–gel transition temperature. The hydrogels exhibit minimal cytotoxicity toward human adipose derived stem cells (hASCs), evidenced from both alamarBlue and PicoGreen assays. Furthermore, quantitative PCR analysis revealed significant up-regulation of the Col2a1 gene and down-regulation of ANGPT1 gene, suggestingmore » that the hydrogel exhibit biological activity in inducing chondrogenesis of hASCs. It was also demonstrated that the hydrogel can be used to quantitatively encapsulate water-soluble enzymes (e.g., horseradish peroxidase) by manipulating the sol–gel transition. The enzymatic activity of HRP remain unperturbed after encapsulation at 37 °C for up to 7 d, suggesting that the hydrogel does not adversely affect the enzyme structure and thereby the enzymatic activity. These results suggest that the polypeptoid hydrogel a promising synthetic platform for tissue engineering or protein storage applications.« less

Authors:
 [1];  [1];  [1];  [1];  [2];  [1];  [2];  [1];  [1]
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  1. Louisiana State Univ., Baton Rouge, LA (United States)
  2. Tulane Univ., New Orleans, LA (United States)
Publication Date:
Research Org.:
Louisiana State Univ., Baton Rouge, LA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1466801
Grant/Contract Number:  
SC0012432
Resource Type:
Accepted Manuscript
Journal Name:
Chemistry of Materials
Additional Journal Information:
Journal Volume: 28; Journal Issue: 3; Journal ID: ISSN 0897-4756
Publisher:
American Chemical Society (ACS)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE

Citation Formats

Xuan, Sunting, Lee, Chang -Uk, Chen, Cong, Doyle, Andrew B., Zhang, Yueheng, Guo, Li, John, Vijay T., Hayes, Daniel, and Zhang, Donghui. Thermoreversible and Injectable ABC Polypeptoid Hydrogels: Controlling the Hydrogel Properties through Molecular Design. United States: N. p., 2015. Web. doi:10.1021/acs.chemmater.5b03528.
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Xuan, Sunting, Lee, Chang -Uk, Chen, Cong, Doyle, Andrew B., Zhang, Yueheng, Guo, Li, John, Vijay T., Hayes, Daniel, & Zhang, Donghui. Thermoreversible and Injectable ABC Polypeptoid Hydrogels: Controlling the Hydrogel Properties through Molecular Design. United States. https://doi.org/10.1021/acs.chemmater.5b03528
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Xuan, Sunting, Lee, Chang -Uk, Chen, Cong, Doyle, Andrew B., Zhang, Yueheng, Guo, Li, John, Vijay T., Hayes, Daniel, and Zhang, Donghui. Mon . "Thermoreversible and Injectable ABC Polypeptoid Hydrogels: Controlling the Hydrogel Properties through Molecular Design". United States. https://doi.org/10.1021/acs.chemmater.5b03528. https://www.osti.gov/servlets/purl/1466801.
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@article{osti_1466801,
title = {Thermoreversible and Injectable ABC Polypeptoid Hydrogels: Controlling the Hydrogel Properties through Molecular Design},
author = {Xuan, Sunting and Lee, Chang -Uk and Chen, Cong and Doyle, Andrew B. and Zhang, Yueheng and Guo, Li and John, Vijay T. and Hayes, Daniel and Zhang, Donghui},
abstractNote = {Here, a series of ABC triblock copolypeptoids [i.e., poly(N-allyl glycine)-b-poly(N-methyl glycine)-b-poly(N-decyl glycine) (AMD)] with well-defined structure and varying composition have been synthesized by sequential primary amine-initiated ring-opening polymerization of the corresponding N-substituted N-carboxyanhydride monomers (Al-NCA, Me-NCA, and De-NCA). The ABC block copolypeptoids undergo sol-to-gel transitions with increasing temperature in water and biological media at low concentrations (2.5–10 wt %). The sol–gel transition is rapid and fully reversible with a narrow transition window, evidenced by the rheological measurements. The gelation temperature (Tgel) and mechanical stiffness of the hydrogels are highly tunable: Tgel in the 26.2–60.0 °C range, the storage modulus (G') and Young’s modulus (E) in the 0.2–780 Pa and 0.5–2346 Pa range, respectively, at the physiological temperature (37 °C) can be readily accessed by controlling the block copolypeptoid composition and the polymer solution concentration. The hydrogel is injectable through a 24 gauge syringe needle and maintains their shape upon in contact with surfaces or water baths that are kept above the sol–gel transition temperature. The hydrogels exhibit minimal cytotoxicity toward human adipose derived stem cells (hASCs), evidenced from both alamarBlue and PicoGreen assays. Furthermore, quantitative PCR analysis revealed significant up-regulation of the Col2a1 gene and down-regulation of ANGPT1 gene, suggesting that the hydrogel exhibit biological activity in inducing chondrogenesis of hASCs. It was also demonstrated that the hydrogel can be used to quantitatively encapsulate water-soluble enzymes (e.g., horseradish peroxidase) by manipulating the sol–gel transition. The enzymatic activity of HRP remain unperturbed after encapsulation at 37 °C for up to 7 d, suggesting that the hydrogel does not adversely affect the enzyme structure and thereby the enzymatic activity. These results suggest that the polypeptoid hydrogel a promising synthetic platform for tissue engineering or protein storage applications.},
doi = {10.1021/acs.chemmater.5b03528},
journal = {Chemistry of Materials},
number = 3,
volume = 28,
place = {United States},
year = {Mon Dec 14 00:00:00 EST 2015},
month = {Mon Dec 14 00:00:00 EST 2015}
}
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https://doi.org/10.1021/acs.chemmater.5b03528
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