PMC:7573174 / 8470-10516 JSONTXT

{"project":"2_test","denotations":[{"id":"33088250-30789273-29803048","span":{"begin":835,"end":837},"obj":"30789273"},{"id":"33088250-27192421-29803049","span":{"begin":1190,"end":1192},"obj":"27192421"},{"id":"33088250-17212393-29803050","span":{"begin":1293,"end":1296},"obj":"17212393"},{"id":"33088250-22309293-29803051","span":{"begin":1567,"end":1569},"obj":"22309293"},{"id":"33088250-31718142-29803052","span":{"begin":1997,"end":1999},"obj":"31718142"},{"id":"33088250-26118539-29803053","span":{"begin":2040,"end":2043},"obj":"26118539"}],"text":"Enzymatic reaction\nEnzymatic reactions, being universal in the biology, are emerging as a powerful trigger for fast and specific assembling processes to generate biomaterials, including hydrogels. For example, enzymatic reactions boost the hydrophobicity of peptide precursors to generate hydrogelators, therefore initiating self-assembly processes. The first example of enzyme-instructed self-assembly (EISA) uses alkaline phosphatase (ALP) to clip off the phosphate group from the precursor (Fmoc-tyrosine phosphate, 2) to form a hydrogelator (3) (Figure 1B(Fig. 1)). Fibrillar networks trap water inside to form a supramolecular hydrogel (Yang et al., 2004[104]). Different from the heat-cooling method, EISA usually gives rise to nanofibers with β-sheet structures, which are essential for receptor recognition (Shang et al., 2019[72]). More importantly, EISA is more compatible to cells than other self-assembly triggers, such heating and cooling.\nBesides ALP, which has a broad spectrum of substrates and fast kinetics, other enzymes, including enterokinase (He et al., 2017[35]), carboxylesterases (CES) (Zhang et al., 2019[112]), matrix metalloproteinases (Kalafatovic et al., 2016[41]), β-galactosidase (Xu et al., 2019[97]; Akama et al., 2018[2]), and β-lactamase (Yang et al., 2007[105]), have acted as the catalysts for EISA. It is also useful to combine enzymatic reaction with fast chemical reactions for EISA. For example, furin-mediated 2-cyanobenzothiazole (CBT) condensation represents a unique strategy to trigger self-assembly (Ghosh et al., 2012[28]). Upon furin clipping off the RVRR sequence from the precursor (4), the exposures of both amine and thiol groups facilitate the condensation reaction with CBT, allow the condensation product to accumulate in the cancer cells that upregulate glutathione (GSH) and furin (Figure 1C(Fig. 1)). This efficient and biocompatible condensation has received extensively exploration in the field of molecular imaging (Wang et al., 2019[78]) and cancer therapy (Yuan et al., 2015[109])."}

{"project":"MyTest","denotations":[{"id":"33088250-30789273-29803048","span":{"begin":835,"end":837},"obj":"30789273"},{"id":"33088250-27192421-29803049","span":{"begin":1190,"end":1192},"obj":"27192421"},{"id":"33088250-17212393-29803050","span":{"begin":1293,"end":1296},"obj":"17212393"},{"id":"33088250-22309293-29803051","span":{"begin":1567,"end":1569},"obj":"22309293"},{"id":"33088250-31718142-29803052","span":{"begin":1997,"end":1999},"obj":"31718142"},{"id":"33088250-26118539-29803053","span":{"begin":2040,"end":2043},"obj":"26118539"}],"namespaces":[{"prefix":"_base","uri":"https://www.uniprot.org/uniprot/testbase"},{"prefix":"UniProtKB","uri":"https://www.uniprot.org/uniprot/"},{"prefix":"uniprot","uri":"https://www.uniprot.org/uniprotkb/"}],"text":"Enzymatic reaction\nEnzymatic reactions, being universal in the biology, are emerging as a powerful trigger for fast and specific assembling processes to generate biomaterials, including hydrogels. For example, enzymatic reactions boost the hydrophobicity of peptide precursors to generate hydrogelators, therefore initiating self-assembly processes. The first example of enzyme-instructed self-assembly (EISA) uses alkaline phosphatase (ALP) to clip off the phosphate group from the precursor (Fmoc-tyrosine phosphate, 2) to form a hydrogelator (3) (Figure 1B(Fig. 1)). Fibrillar networks trap water inside to form a supramolecular hydrogel (Yang et al., 2004[104]). Different from the heat-cooling method, EISA usually gives rise to nanofibers with β-sheet structures, which are essential for receptor recognition (Shang et al., 2019[72]). More importantly, EISA is more compatible to cells than other self-assembly triggers, such heating and cooling.\nBesides ALP, which has a broad spectrum of substrates and fast kinetics, other enzymes, including enterokinase (He et al., 2017[35]), carboxylesterases (CES) (Zhang et al., 2019[112]), matrix metalloproteinases (Kalafatovic et al., 2016[41]), β-galactosidase (Xu et al., 2019[97]; Akama et al., 2018[2]), and β-lactamase (Yang et al., 2007[105]), have acted as the catalysts for EISA. It is also useful to combine enzymatic reaction with fast chemical reactions for EISA. For example, furin-mediated 2-cyanobenzothiazole (CBT) condensation represents a unique strategy to trigger self-assembly (Ghosh et al., 2012[28]). Upon furin clipping off the RVRR sequence from the precursor (4), the exposures of both amine and thiol groups facilitate the condensation reaction with CBT, allow the condensation product to accumulate in the cancer cells that upregulate glutathione (GSH) and furin (Figure 1C(Fig. 1)). This efficient and biocompatible condensation has received extensively exploration in the field of molecular imaging (Wang et al., 2019[78]) and cancer therapy (Yuan et al., 2015[109])."}