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|a pubmed24n1435.xml
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|a (DE-627)NLM262809737
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|a (NLM)27458325
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Xuan, Sunting
|e verfasserin
|4 aut
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|a Thermoreversible and Injectable ABC Polypeptoid Hydrogels
|b Controlling the Hydrogel Properties through Molecular Design
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|c 2016
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Revised 10.06.2024
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a 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
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|a Journal Article
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|a Lee, Chang-Uk
|e verfasserin
|4 aut
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|a Chen, Cong
|e verfasserin
|4 aut
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|a Doyle, Andrew B
|e verfasserin
|4 aut
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|a Zhang, Yueheng
|e verfasserin
|4 aut
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|a Guo, Li
|e verfasserin
|4 aut
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|a John, Vijay T
|e verfasserin
|4 aut
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|a Hayes, Daniel
|e verfasserin
|4 aut
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|a Zhang, Donghui
|e verfasserin
|4 aut
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|i Enthalten in
|t Chemistry of materials : a publication of the American Chemical Society
|d 1998
|g 28(2016), 3 vom: 09. Feb., Seite 727-737
|w (DE-627)NLM098194763
|x 0897-4756
|7 nnns
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|g volume:28
|g year:2016
|g number:3
|g day:09
|g month:02
|g pages:727-737
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|d 28
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|h 727-737
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