A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Coating Nanoparticles with Plant-Produced Transferrin-Hydrophobin Fusion Protein Enhances Their Uptake in Cancer Cells
Tekijät: Reuter LJ, Shahbazi MA, Makila EM, Salonen JJ, Saberianfar R, Menassa R, Santos HA, Joensuu JJ, Ritala A
Kustantaja: AMER CHEMICAL SOC
Julkaisuvuosi: 2017
Journal: Bioconjugate Chemistry
Tietokannassa oleva lehden nimi: BIOCONJUGATE CHEMISTRY
Lehden akronyymi: BIOCONJUGATE CHEM
Vuosikerta: 28
Numero: 6
Aloitussivu: 1639
Lopetussivu: 1648
Sivujen määrä: 10
ISSN: 1043-1802
DOI: https://doi.org/10.1021/acs.bioconjchem.7b00075
Tiivistelmä
The encapsulation of drugs to nanoparticles may offer a solution for targeted delivery. Here, we set out to engineer a self assembling targeting ligand by combining the functional properties of human transferrin and fungal hydrophobins in a single fusion protein. We showed that human transferrin can be expressed in Nicotiana benthamiana plants as a fusion with Trichoderma reesei hydrophobins HFBI, HFBII, or HFBIV. Transferrin-HFBIV was further expressed in tobacco BY-2 suspension cells. Both partners of the fusion protein retained their functionality; the hydrophobin moiety enabled migration to a surfactant phase in an aqueous two-phase system, and the transferrin moiety was able to reversibly bind iron. Coating porous silicon nanoparticles with the fusion protein resulted in uptake of the nanoparticles in human cancer cells. This study provides a proof-of concept for the functionalization of hydrophobin coatings with transferrin as a targeting ligand.
The encapsulation of drugs to nanoparticles may offer a solution for targeted delivery. Here, we set out to engineer a self assembling targeting ligand by combining the functional properties of human transferrin and fungal hydrophobins in a single fusion protein. We showed that human transferrin can be expressed in Nicotiana benthamiana plants as a fusion with Trichoderma reesei hydrophobins HFBI, HFBII, or HFBIV. Transferrin-HFBIV was further expressed in tobacco BY-2 suspension cells. Both partners of the fusion protein retained their functionality; the hydrophobin moiety enabled migration to a surfactant phase in an aqueous two-phase system, and the transferrin moiety was able to reversibly bind iron. Coating porous silicon nanoparticles with the fusion protein resulted in uptake of the nanoparticles in human cancer cells. This study provides a proof-of concept for the functionalization of hydrophobin coatings with transferrin as a targeting ligand.
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