Design of antibacterial biointerfaces by surface modification of poly (ε-caprolactone) with fusion protein containing hydrophobin and PA-1.
Design of antibacterial biointerfaces by surface modification of poly (ε-caprolactone) with fusion protein containing hydrophobin and PA-1.
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DOI:
10.1016/j.colsurfb.2016.12.019
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发表时间:
2017-03
期刊:
影响因子:
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通讯作者:
Xiangxiang Wang;Jiwei Mao;Yiming Chen;Dongmin Song;Zhendong Gao;Xiuming Zhang;Yanling Bai;P. Saris;H. Feng;Haijin Xu;M. Qiao
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文献类型:
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作者:
Xiangxiang Wang;Jiwei Mao;Yiming Chen;Dongmin Song;Zhendong Gao;Xiuming Zhang;Yanling Bai;P. Saris;H. Feng;Haijin Xu;M. Qiao
Class IIa bacteriocin pediocin PA-1 has broad-spectrum activity and is a well-characterized candidate food biopreservative. Here, a simple approach is designed to extend the application of pediocin PA-1 in improving the antibacterial activity of electrospun poly(caprolactone) (PCL) grafts through combining PA-1 with HGFI, which is a self-assembled protein with characteristics allowing the modulation of surface properties of other materials originated fromGrifola frondosa.Saccharomyces cerevisiaewas used as the host for expression of fusion protein PA-1-linker-HGFI (pH) and his-tag purification was used to purify recombinant protein pH. An antibacterial activity assay showed the fusion protein pH retained the biological property of native PA-1. Water contact angle, X-ray photoelectron spectroscopy, immunofluorescence assay and atomic force microscopy indicated the surface properties of HGFI were greatly preserved by the fusion protein pH. Finally, antibacterial activity of pH-modified PCL substrate measurements implied the fusion protein significantly improved the bacterial-resistance of the PCL film through dressing the PCL fibers with the recombinant pH protein. This work presents a new perspective on the application of hydrophobin and pediocin PA-1 in antibacterial medical devices.