2016
DOI: 10.1021/acsami.5b09633
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Multifunctional Polyphenols- and Catecholamines-Based Self-Defensive Films for Health Care Applications

Abstract: In an era of relentless evolution of antimicrobial resistance, there is an increasing demand for the development of efficient antimicrobial coatings or surfaces for food, biomedical, and industrial applications. This study reports the laccase-catalyzed room-temperature synthesis of mechanically robust, thermally stable, broad spectrum antimicrobial films employing interfacial interactions between poly(vinyl alcohol), PVA, and 14 naturally occurring catecholamines and polyphenols. The oxidative products of cate… Show more

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Cited by 77 publications
(56 citation statements)
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“…Compared with organic fouling, membrane fouling caused by microorganisms is more challenging because of the formation of biofilms and extracellular polymeric substances . It is well known that TA is an effective natural antimicrobial agent that is capable of inactivating these microorganisms through the chelating of Ca 2+ and Mg 2+ on the outer membrane, the disordering of the electrical balance, and ultimately, the damage of the cellular membrane structure. We estimated that the TA‐modified membrane surface may have been able to exhibit antibiofouling properties, including anti‐attachment and/or inactivation of the adhered microorganisms.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Compared with organic fouling, membrane fouling caused by microorganisms is more challenging because of the formation of biofilms and extracellular polymeric substances . It is well known that TA is an effective natural antimicrobial agent that is capable of inactivating these microorganisms through the chelating of Ca 2+ and Mg 2+ on the outer membrane, the disordering of the electrical balance, and ultimately, the damage of the cellular membrane structure. We estimated that the TA‐modified membrane surface may have been able to exhibit antibiofouling properties, including anti‐attachment and/or inactivation of the adhered microorganisms.…”
Section: Resultsmentioning
confidence: 99%
“…Bacteria‐induced biofouling was performed with Escherichia coli K1 ( E. coli K1) as the typical bacterial strain. The bacterial suspension was prepared with typical methods with slight modification as summarized here. A single colony of E. coli K1 was isolated from streak plates, then dispersed in 10 mL of fresh Luria‐Bertani broth, and cultivated in incubator (37 °C) under shaking for 18 h. After that, 200 μL of the inoculum was transferred into fresh broth, incubated for 2 h, and harvested in the mid‐log‐phase period.…”
Section: Methodsmentioning
confidence: 99%
“…Our results do suggest that, depending on the intensity of the oxidative reaction, chemically-distinct, dark-or light-colored MN-like pigments could be generated depending on the type of precursor that is present. Such physically and chemically distinct MN materials could find different applications 7,16,[43][44][45][46] or possess different cell-biological properties [47][48][49][50][51][52] In addition, our results suggest that the absence of a dark color does not necessarily mean the absence of MN-like materials which may have implications for the evaluation of histological or fossil specimens. [53][54] …”
Section: 323uv-vis Spectroscopy and Fluorescence Emissionmentioning
confidence: 89%
“…Enzyme Catalyzed Oxidation : The natural formation of eumelanins involves the tyrosinase‐catalyzed oxidation of l ‐tyrosine, ultimately to DHI and 5,6‐dihydroxyindole‐2‐carboxylic acid and their quinone analog starting materials . Similarly, enzymes can be used to catalyze the oxidative polymerization of catecholamines . For example, laccase and tyrosinase have each been used to activate the catechol groups of a range of catecholamines for subsequent polymerization, with laccase also promoting polymerization under acidic conditions .…”
Section: Catecholamine Polymers: Chemistry and Structurementioning
confidence: 99%
“…Similarly, enzymes can be used to catalyze the oxidative polymerization of catecholamines . For example, laccase and tyrosinase have each been used to activate the catechol groups of a range of catecholamines for subsequent polymerization, with laccase also promoting polymerization under acidic conditions . Further, DHI, l ‐DOPA, and dopamine have all been used to make coatings in the presence of hydrogen peroxide and horse radish peroxidase, the enzyme catalyzing the reaction as no observable coating occurred with just the peroxide in solution.…”
Section: Catecholamine Polymers: Chemistry and Structurementioning
confidence: 99%