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:
Colloids and surfaces. B, Biointerfaces
影响因子:
--
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
Xiangxiang Wang;Jiwei Mao;Yiming Chen;Dongmin Song;Zhendong Gao;Xiuming Zhang;Yanling Bai;P. Saris;H. Feng;Haijin Xu;M. Qiao
中科院分区:
其他
文献类型:
--
作者:
Xiangxiang Wang;Jiwei Mao;Yiming Chen;Dongmin Song;Zhendong Gao;Xiuming Zhang;Yanling Bai;P. Saris;H. Feng;Haijin Xu;M. Qiao

文献摘要

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IIa类细菌素pediocin PA-1具有广谱活性,是一种具有良好特性的候选食品生物防腐剂。本研究设计了一种简单的方法来扩展pediocin PA-1在提高静电纺丝聚乳酸抗菌活性方面的应用通过将PA-1与HGFI结合,该融合蛋白PA-1-linker-HGFI(pH)是一种自组装蛋白,具有调节其它灰树花材料表面性质的特性。抗菌活性检测表明,融合蛋白pH值保持了天然PA-1的生物学特性。水接触角、X射线光电子能谱、免疫荧光分析和原子力显微镜观察表明,HGFI的表面性质被融合蛋白的pH值大大保留。最后,pH值修饰的PCL基底的抗菌活性测量表明,融合蛋白通过将重组pH值蛋白修饰在PCL纤维上,显著提高了PCL膜的抗菌性。本研究为疏水蛋白和抗菌肽PA-1在抗菌医疗器械中的应用提供了新的视角。
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.