2010
DOI: 10.1016/j.bios.2010.08.059
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Hydrophilic modification of polystyrene with hydrophobin for time-resolved immunofluorometric assay

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Cited by 45 publications
(33 citation statements)
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“…The oldest processes are wet chemical techniques. [16][17][18][19][20] Polystyrene functionalization employing atomic oxygen treatments 17,21 is a well-documented example of such wet chemistry approaches. However, the complex downstream treatment of costly and sometimes hazardous solvents hinders the application of wet chemistry approaches on a larger scale.…”
Section: Introductionmentioning
confidence: 99%
“…The oldest processes are wet chemical techniques. [16][17][18][19][20] Polystyrene functionalization employing atomic oxygen treatments 17,21 is a well-documented example of such wet chemistry approaches. However, the complex downstream treatment of costly and sometimes hazardous solvents hinders the application of wet chemistry approaches on a larger scale.…”
Section: Introductionmentioning
confidence: 99%
“…Most importantly, a discrete portion of their exposed surface is composed of amino acids with hydrophobic sidechains; this hydrophobic patch endows hydrophobins with exceptional amphiphilic properties and drives their spontaneous and rapid self-assembly at hydrophobic/hydrophilic interfaces, such as air/water and oil/water boundaries, where they pack into ordered structures and form remarkably strong and elastic fi lms. [ 22,23 ] Hydrophobins also effi ciently assemble onto solid surfaces to form amphiphilic fi lms that are able to reverse the surface wettability of the coated material [ 24 ] and allow for the immobilization of, e.g., proteins or enzymes onto solid surfaces [25][26][27][28] while preserving all of the features of the immobilized biomolecules. [ 29 ] The main advantage of this method is its simplicity: hydrophobin self-assembly proceeds spontaneously at room temperature within seconds or minutes and requires only a very tiny amount of protein.…”
Section: Introductionmentioning
confidence: 99%
“…In contrast, biomolecules have less conformational change and retain functional activity when are immobilized on hydrophilic surfaces, as the major driving force between biomolecules and the hydrophilic surface is the electrostatic force (Goddard and Hotchkiss, 2007;Kaur et al, 2004;Lubarsky et al, 2005). Moreover the strength and selectivity of protein-protein interactions make proteins excellent candidates to serve as linkers to form ordered structures (Wang 2010). Taking into consideration the above mentioned evidences, self assembling proteins like hydrophobins that have the remarkable property of adhering to almost any surface forming stable amphiphylic films are very good candidates to easily manufacture stable, enzymebased catalytic surfaces for applications in biosensing.…”
Section: Biosensors Based On Organic/inorganic Interfacesmentioning
confidence: 99%
“…In particular, time resolved fluorescence assay has been used for the quantitative determination of carcinoembryonic antigen. A detection limit of 0.24 ng/mL is claimed by authors (Wang et al 2010). Even if class II is less chemically stable, HFBI has been used in glucose biosensing once decorated by multi wall carbon nanotube and glucose oxidase (Wang et al 2010).…”
mentioning
confidence: 99%
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