Functional modification of poly(ε-caprolactone)with fusion protein containing HGFI and PA-1 improved

来源 :中国生物化学与分子生物学会2016年全国学术会议 | 被引量 : 0次 | 上传用户:yinzheng1974
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  Pediocin PA-1 is the most extensively studied class Ⅱa bacteriocin,which shows a broad-spectrum activity and has been well characterized to be applied as a food biopreservative.Herein,an easy-to-do approach is designed to extend the application of pediocin PA-1 in improving antibacterial activity of electrospun PCL grafts through combining PA-1 with HGFI,a kind of self-assembled protein displaying unique characteristics to change surface properties of other materials originated from Grifola frondosa.Saccharomyces cerevisiae was used as the host for the expression of the fusion protein PA-1-linker-HGFI(PH)and his-tag purification technique was used to purify recombinant protein PH.Antibacterial activity assay showed that fusion protein PH has retained the featured biological property of native PA-1.Water contact angle(WCA),scanning electron microscope(SEM),X-ray photoelectron spectroscopy(XPS)and immunofluorescence assay indicated that the surface properties of HGFI were greatly preserved by the fusion protein PH.At last,antibacterial activity of PH modiying PCL substrates measurement implied that the fusion protein significantly improved the bacterial-resistant ability of PCL film through dressing the PCL fibers with “PA-1 logo clothes”.This work presented a new perspective to apply hydrophobin and pediocin PA-1 in bacterial-free medical devices.
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