Publications by authors named "Ming-qiang Qiao"

Surface wettability conversion with hydrophobins is important for its applications in biodevices. In this work, the application of a type I hydrophobin HGFI in surface wettability conversion on mica, glass, and poly(dimethylsiloxane) (PDMS) was investigated. X-ray photoelectron spectroscopy (XPS) and water-contact-angle (WCA) measurements indicated that HGFI modification could efficiently change the surface wettability.

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Article Synopsis
  • Hydrophobins are small proteins from fungi that can alter surface wettability by self-assembling into films; for example, the hydrophobin HFBI reduced the water contact angle on gold from approximately 73.8 degrees to 45.3 degrees.
  • A quartz crystal microbalance analysis showed a coverage density of 588 ng/cm² for HFBI on gold, and the film remained stable across a wide pH range (1 to 13).
  • The HFBI-modified gold surface successfully immobilized the enzyme choline oxidase (ChOx), leading to a highly responsive amperometric biosensor capable of generating a significant output current, indicating its potential for effective electrochemical biosensing.
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Contributions of the evolutionarily conserved A16Leu and B17Leu to insulin foldability were characterized by evaluating folding properties of single-chain insulin analogs. The results showed A16Leu had much more significant effects on the foldability of insulin than B17Leu.

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Protein immobilization is a crucial step in protein chip, biosensor, etc. Here, two methods to immobilize proteins on glass surface were analyzed, one is silanization method using 3-aminopropyltriethoxysilane (APTES), and the other is hydrophobin HFBI coating. The modified glass surfaces were characterized with X-ray photoelectron spectroscopy (XPS), water contact angle measurement (WCA) and immunoassay.

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Bioactive surfaces with appropriate hydrophilicity for protein immobilization can be achieved by hydrophobin II (HFBI) self-assembly on mica and polydimethylsiloxane (PDMS) surfaces. X-ray photoelectron spectroscopy and water contact angle measurements illustrated that the surface wettability can be changed from superhydrophobic (PDMS) or superhydrophilic (mica) to moderately hydrophilic, which is suitable for protein (chicken IgG) immobilization on both substrate surfaces. The results suggest that HFBI assembly, one kind of hydrophobin from Trichoderma reesei, may be a versatile and convenient method for the immobilization of biomolecules on diverse substrates, which may have potential applications in biosensors, immunoassays, and microfluidic networks.

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Hydrophobins are a family of natural self-assembling proteins with high biocompability, which are apt to form strong and ordered assembly onto many kinds of surfaces. These physical-chemical and biological properties make hydrophobins suitable for surface modification and biomolecule immobilization purposes. A class II hydrophobin HFBI was used as enzyme immobilization matrix on platinum electrode to construct amperometric glucose biosensor.

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Pseudomonas aeruginosa, a typical opportunistic pathogen, has a single polar flagella which provides swimming motility and virulence. Twelve of insertional mutants with Mu transposition complexes into genomic DNA of Pseudomonas aeruginosa were screened on the changes of swimming motility. After gene cloning and DNA sequencing of those mutants, ten of them were illustrated that defective mutations on swimming motility were caused by insertions of Mu transposon into 10 of different functional genes which may involved in biosynthesis of flagella and gene regulations, but another two mutants were resulted from the insertion of two new genes (PA2950, PA5022) with function unknown.

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S1 nuclease (from Aspergillus oryzae) is a specific enzyme to degrade single stranded DNA or RNA molecules. It has been reported to be able to convert superhelical circular DNA molecules into open circle or linear forms under certain conditions, but this function has not been well explored. In order to use the action of S1 nuclease to linearize circular DNA and develop a novel way of cloning microcircular DNAs, the pUC19 was used to investigate the relationship between the linearization efficiency of S1 nuclease and the amount of enzyme used.

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Mu transposition recombination technique was firstly used as a mutagenesis tool to explore a cluster of genes involved in biosynthesis and regulation of pigments in P. aeruginosa. Eight pigment mutants were screened and identified.

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A P. aeruginosa strain PA68 isolated from the sputum of a patient suffering from bronchiectasis was used as the recipient strain. Optimum conditions including growth stage of the strain, electroshock voltage, concentration and preservation of competent cell were defined for the electroporation of PA68 with plasmid pSMC28.

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