2017
DOI: 10.1002/bip.23077
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Enhanced tissue adhesiveness of injectable gelatin hydrogels through dual catalytic activity of horseradish peroxidase

Abstract: Development of bioadhesives with tunable mechanical strength, high adhesiveness, biocompatibility, and injectability is greatly desirable in all surgeries to replace or complement the sutures and staples. Herein, the dual catalytic activity of horseradish peroxidase is exploited to in situ form the hydroxyphenyl propionic acid-gelatin/thiolated gelatin (GH/GS) adhesive hydrogels including two alternative crosslinks (phenol-phenol and disulfide bonds) with fast gelation (few seconds -several minutes) and improv… Show more

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Cited by 32 publications
(15 citation statements)
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“…Thi et al fabricated a gelatin-based hydrogel with dual cross-linking functionality by mixing hydroxyphenyl propionic acid-modified gelatin (GH) with thiolated gelatin (GS). 284 GH was cross-linked with HRP/H 2 O 2 , and the adhesive strength of the hydrogel increased 6-fold upon addition of GS due to the formation of disulfide cross-links within the hydrogel and at the hydrogel-tissue interface. 284 Engineered polypeptides have also been designed to form hydrogels via disulfide bonds.…”
Section: Disulfide Cross-linkingmentioning
confidence: 99%
See 1 more Smart Citation
“…Thi et al fabricated a gelatin-based hydrogel with dual cross-linking functionality by mixing hydroxyphenyl propionic acid-modified gelatin (GH) with thiolated gelatin (GS). 284 GH was cross-linked with HRP/H 2 O 2 , and the adhesive strength of the hydrogel increased 6-fold upon addition of GS due to the formation of disulfide cross-links within the hydrogel and at the hydrogel-tissue interface. 284 Engineered polypeptides have also been designed to form hydrogels via disulfide bonds.…”
Section: Disulfide Cross-linkingmentioning
confidence: 99%
“…284 GH was cross-linked with HRP/H 2 O 2 , and the adhesive strength of the hydrogel increased 6-fold upon addition of GS due to the formation of disulfide cross-links within the hydrogel and at the hydrogel-tissue interface. 284 Engineered polypeptides have also been designed to form hydrogels via disulfide bonds. Shen et al designed am artificial protein cross-linked by leucine zipper domains.…”
Section: Disulfide Cross-linkingmentioning
confidence: 99%
“…Similarly, other hydrogels were formed; the specific formulations and corresponding code are presented in Table 3. The time when the mixtures stopped flowing was recorded as the gelation time [30,31]. Each sample was triplicated to calculate the average value and standard deviation.…”
Section: Hydrogel Formation and Characterizationmentioning
confidence: 99%
“…Recently, there has been growing interest in creating in situ cross-linkable hydrogels through enzymatic reaction because of the hydrogel formation in physiological conditions and substrate-specific conjugations. Several types of enzyme-mediated cross-linkable hydrogels have been developed using several enzymes [e.g., horseradish peroxidase (HRP), transglutaminase, tyrosinase, lysyl oxidase, and laccase (Lac)] [15][16][17][34][35][36][37][38][39]. Specifically, HRP-mediated cross-linking reactions have attracted attention as a promising chemical cross-linking method because of the biocompatibility and easily controllable physicochemical and biological properties of the hydrogels (e.g., gelation kinetics, mechanical strength, and degradation behaviors) [40,41].…”
Section: Strategies To Fabricate In Situ Cross-linkable Hydrogelsmentioning
confidence: 99%