Hao Xie
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Hao Xie has a total of 132 co-authors. Here are the top co-authors by number of shared publications:
- Hang Ping
State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, Luoshi Road No. 122, Wuhan 430070, China
18 shared publications - Zhengyi Fu
Wuhan University of Technology
16 shared publications - Bao-Lian Su
State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, Wuhan, Hubei 430070, China
10 shared publications Weimin Wang
State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, Wuhan University of Technology, Wuhan, 430070, China
8 shared publicationsWeijian Fang
Hubei Longzhong Laboratory, Wuhan University of Technology Xiangyang Demonstration Zone, Xiangyang 441000, China
7 shared publications- Junhui Guo
School of Chemistry, Chemical Engineering and Life Sciences, Wuhan University of Technology, Wuhan 430070, China
6 shared publications
Latest Publications
- 22 April 2026
- Published by Elsevier in Colloids and Surfaces B: Biointerfaces
- Vol. 265, 115727
A Shikonin-loaded smart dressing integrating self-adaptive release, visual monitoring, and enhanced healing for diabetic wounds
- 22 April 2026
- Published by Elsevier in Colloids and Surfaces B: Biointerfaces
- Vol. 265, 115727
A Shikonin-loaded smart dressing integrating self-adaptive release, visual monitoring, and enhanced healing for diabetic wounds
- 9 April 2026
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
Mineralization of Bouligand-structured collagen matrices derived from fish scales with enhanced mechanical properties and biocompatibility
After demineralization, jiangjunjia scales used as collagen scaffolds retain their Bouligand structure and internal collagen fiber morphology. After remineralization, they exhibit excellent mechanical properties and biocompatibility.
- 9 April 2026
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
Mineralization of Bouligand-structured collagen matrices derived from fish scales with enhanced mechanical properties and biocompatibility
After demineralization, jiangjunjia scales used as collagen scaffolds retain their Bouligand structure and internal collagen fiber morphology. After remineralization, they exhibit excellent mechanical properties and biocompatibility.
- 31 October 2024
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
- Vol. 13 (1) , 312-325
Intrafibrillar calcium carbonate mineralization of electrospinning polyvinyl alcohol/collagen films with improved mechanical and bioactive properties
The mineralized PVA/Col–CaCO3 film play an essential role in guided bone-regeneration (GBR) techniques, which exhibited good mechanical and bioactive properties.
- 31 October 2024
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
- Vol. 13 (1) , 312-325
Intrafibrillar calcium carbonate mineralization of electrospinning polyvinyl alcohol/collagen films with improved mechanical and bioactive properties
The mineralized PVA/Col–CaCO3 film play an essential role in guided bone-regeneration (GBR) techniques, which exhibited good mechanical and bioactive properties.
- 1 June 2023
- Published by Springer Nature in Journal of Wuhan University of Technology-Mater. Sci. Ed.
- Vol. 38 (4) , 924-928
A Preliminary Study of Cell Membrane Mediated Immobilization of a Recombinant Acyl-homoserine Lactonase AidH
- 1 June 2023
- Published by Springer Nature in Journal of Wuhan University of Technology-Mater. Sci. Ed.
- Vol. 38 (4) , 924-928
A Preliminary Study of Cell Membrane Mediated Immobilization of a Recombinant Acyl-homoserine Lactonase AidH
- 5 January 2023
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - General Subjects
- Vol. 1867 (3) , 130305
Molecular mechanism of lipopolysaccharide (LPS) in promoting biomineralization on bacterial surface
- 5 January 2023
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - General Subjects
- Vol. 1867 (3) , 130305
Molecular mechanism of lipopolysaccharide (LPS) in promoting biomineralization on bacterial surface
- Open Access
- 10 August 2022
- Published by Royal Society of Chemistry (RSC) in RSC Advances
- Vol. 12 (35) , 22695-22702
Multiple fluorescence response behaviours to proteins/bacteria and selective antibacterial activity of cetylpyridinium chloride (CPC)-based cationic carbon dots
Direct interaction between carbon dots (CDs) and biomolecules leads to changes in the chemical and physical status as well as properties of CDs, which can have various biological and biomedical applications. In this work, the surface of CDs was modified with cetylpyridinium chloride (CPC) to facilitate interactions between CDs and biomolecules. Multiple fluorescence response behaviours of CPC-based CDs were observed towards several proteins (bovine serum albumin, lysozyme, protamine, and hemoglobin) and bacterial cells (Escherichia coli and Staphylococcus aureus). Electrostatic attraction and hydrogen bonding were involved in inducing aggregation of CDs and fluorence enhancement. An inner filter effect might also occur to reduce fluorescence of CDs when interacting with proteins. Selective antibacterial activity of CPC-based CDs was observed towards Gram positive bacterium Staphylococcus aureus. This work provides potential to develop CD-based techniques for detecting and visualizing proteins/bacteria as well as selective antibacterial agents towards Gram-positive bacteria.
- 10 August 2022
- Published by Royal Society of Chemistry (RSC) in RSC Advances
- Vol. 12 (35) , 22695-22702
Open AccessMultiple fluorescence response behaviours to proteins/bacteria and selective antibacterial activity of cetylpyridinium chloride (CPC)-based cationic carbon dots
Direct interaction between carbon dots (CDs) and biomolecules leads to changes in the chemical and physical status as well as properties of CDs, which can have various biological and biomedical applications. In this work, the surface of CDs was modified with cetylpyridinium chloride (CPC) to facilitate interactions between CDs and biomolecules. Multiple fluorescence response behaviours of CPC-based CDs were observed towards several proteins (bovine serum albumin, lysozyme, protamine, and hemoglobin) and bacterial cells (Escherichia coli and Staphylococcus aureus). Electrostatic attraction and hydrogen bonding were involved in inducing aggregation of CDs and fluorence enhancement. An inner filter effect might also occur to reduce fluorescence of CDs when interacting with proteins. Selective antibacterial activity of CPC-based CDs was observed towards Gram positive bacterium Staphylococcus aureus. This work provides potential to develop CD-based techniques for detecting and visualizing proteins/bacteria as well as selective antibacterial agents towards Gram-positive bacteria.
- 10 January 2022
- Published by Elsevier in Colloids and Surfaces B: Biointerfaces
- Vol. 211, 112331
Lipopolysaccharide-stabilized ionic colloids induce biomineralization
- 10 January 2022
- Published by Elsevier in Colloids and Surfaces B: Biointerfaces
- Vol. 211, 112331
Lipopolysaccharide-stabilized ionic colloids induce biomineralization
- 10 October 2021
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
- Vol. 9 (44) , 9136-9141
Silk fibroin directs the formation of monetite nanocrystals and their assembly into hierarchical composites
A gel-like silk film is used as the substrate to regulate the formation of monetite with hierarchical structure. The silk film not only changed the crystallization pathway, but also significantly modified the morphology of the crystals.
- 10 October 2021
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
- Vol. 9 (44) , 9136-9141
Silk fibroin directs the formation of monetite nanocrystals and their assembly into hierarchical composites
A gel-like silk film is used as the substrate to regulate the formation of monetite with hierarchical structure. The silk film not only changed the crystallization pathway, but also significantly modified the morphology of the crystals.
- 15 September 2021
- Published by Springer Nature in Applied Biochemistry and Biotechnology
- Vol. 194 (2) , 737-747
Functional Immobilization of a Biofilm-Releasing Glycoside Hydrolase Dispersin B on Magnetic Nanoparticles
Dispersin B (DspB) is a member of glycoside hydrolase family 20 (GH20) and catalyzes degradation of biofilms forming by pathogenic bacteria such as Staphylococcus aureus. Magnetoreceptor (MagR) is a magnetic protein that can be used as a fusion partner for functionally immobilizing proteins on magnetic surfaces. In the present study, a recombinant protein DspB-MagR was constructed by fusing MagR to the C-terminus of DspB and expressed in Escherichia coli. Magnetic immobilization of purified DspB-MagR on magnetic core–shell structured Fe3O4@SiO2 nanoparticles was achieved and characterized by means of various techniques including SDS-PAGE, Fourier transform infrared spectroscopy, thermogravimetric analysis, zeta potential measurement, and scanning electron microscopy. It was evaluated the influence of temperature, pH, and storage time on the performance of immobilized DspB-MagR on Fe3O4@SiO2 nanoparticles. Removal of biofilms forming by Staphylococcus aureus and other medical sourced bacterial species was achieved by using Fe3O4@SiO2 nanoparticles loading with DspB-MagR. This work promoted potential applications of DspB and similar enzymes for medical purposes.
- 15 September 2021
- Published by Springer Nature in Applied Biochemistry and Biotechnology
- Vol. 194 (2) , 737-747
Functional Immobilization of a Biofilm-Releasing Glycoside Hydrolase Dispersin B on Magnetic Nanoparticles
Dispersin B (DspB) is a member of glycoside hydrolase family 20 (GH20) and catalyzes degradation of biofilms forming by pathogenic bacteria such as Staphylococcus aureus. Magnetoreceptor (MagR) is a magnetic protein that can be used as a fusion partner for functionally immobilizing proteins on magnetic surfaces. In the present study, a recombinant protein DspB-MagR was constructed by fusing MagR to the C-terminus of DspB and expressed in Escherichia coli. Magnetic immobilization of purified DspB-MagR on magnetic core–shell structured Fe3O4@SiO2 nanoparticles was achieved and characterized by means of various techniques including SDS-PAGE, Fourier transform infrared spectroscopy, thermogravimetric analysis, zeta potential measurement, and scanning electron microscopy. It was evaluated the influence of temperature, pH, and storage time on the performance of immobilized DspB-MagR on Fe3O4@SiO2 nanoparticles. Removal of biofilms forming by Staphylococcus aureus and other medical sourced bacterial species was achieved by using Fe3O4@SiO2 nanoparticles loading with DspB-MagR. This work promoted potential applications of DspB and similar enzymes for medical purposes.
- 22 July 2021
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
- Vol. 9 (33) , 6668-6677
Growth of mineralized collagen films by oriented calcium fluoride nanocrystal assembly with enhanced cell proliferation
The intrafibrillar mineralization of collagen films with oriented calcium fluoride nanocrystals in vitro is realized. The growth process of the mineralized collagen films is revealed and they exhibit an enhanced cell proliferation.
- 22 July 2021
- Published by Royal Society of Chemistry (RSC) in Journal of Materials Chemistry B
- Vol. 9 (33) , 6668-6677
Growth of mineralized collagen films by oriented calcium fluoride nanocrystal assembly with enhanced cell proliferation
The intrafibrillar mineralization of collagen films with oriented calcium fluoride nanocrystals in vitro is realized. The growth process of the mineralized collagen films is revealed and they exhibit an enhanced cell proliferation.