Development of tumor targeting PHBHHx nanoparticles by PhaP mediated immobilization of EGFR-targeting peptide.

Fan FAN; Jiangang MA; Xiaoyun LU; Teng NIU; Zhimin WU

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Development of tumor targeting PHBHHx nanoparticles by PhaP mediated immobilization of EGFR-targeting peptide.

Author: Fan FAN ¹ ; Jiangang MA ¹ ; Xiaoyun LU ¹ ; Teng NIU ¹ ; Zhimin WU ¹
Author Information

1. Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi'an Jiaotong University, Xi'an 710049, Shaanxi, China.
Publication Type:Journal Article
Keywords: EGFR; PHBHHx; PhaP; drug delivery carrier; tumor targeting
From: Chinese Journal of Biotechnology 2017;33(6):1028-1036
CountryChina
Language:Chinese
Abstract: PHA granule binding protein phasin (PhaP) has a high affinity for hydrophobic materials and can bind to hydrophobic polymers via strong hydrophobic interaction. In this study, an EGFR-targeting peptide (ETP) was fused with PhaP and the fusion protein ETP-PhaP was produced in recombinant Escherichia coli BL21 (DE3) (pPI-ETP-P) and then purified by Ni affinity purification. The tumor targeting PHBHHx nanoparticles were developed based on PhaP mediated ETP immobilization and the cellular uptake of the ETP-PhaP modified PHBHHx NPs and none modified PHBHHx NPs by cervical cancer cell lines SiHa (EGFR over expressed) and CaSKi (EGFR low expressed) were analyzed. The purified ETP-PhaP could be adsorbed onto the hydrophobic surface of PHBHHx NPs. The ETP-PhaP modified PHBHHx NPs could target to EGFR over expressed cervical cancer cells SiHa more efficiently than to the EGFR low expressed CaSKi cells. These results demonstrated the advantage in effectiveness and convenience of PhaP mediated ETP adsorption on PHBHHx nanoparticles, providing a novel strategy for hydrophobic nanocarrier surface modification.