Tumor-Penetrating Peptide-Functionalized Ferritin
Enhances Antitumor Activity of Paclitaxel
Posted on 2021-02-18 - 17:12
We
describe the development of a neuropilin-1 binding peptide (RGERPPR)-ferritin
nanocage that specifically targets tumor cells. Herein, the tumor-penetrating
peptide RGERPPR motif was modified at the C-terminal of human H chain
ferritin (HFtn) using flexible linker moieties. Since the C-terminal
of HFtn is positioned toward the inner cavity, relatively long linkers
(GGGGS)4 were used, in which the MMP-2 cleavage site was
inserted in the linker. The RGERPPR motif was proved to be exposed
outside the protein shell by the effective cleavage at the linker
region by MMP-2. The loading of paclitaxel (PTX) and HFtn-mMMP2-RGE
was prepared by using the low concentration of urea. In vitro studies demonstrated that HFtn-mMMP2-RGE-PTX nanoparticles exhibited
better cytotoxicity and could specifically bind to and be taken up
by human lung cancer cells A549 that highly express NRP-1 receptor.
Better penetrability and growth inhibitory effect were also verified
by the 3D tumor spheroid experiment. The results confirmed that the
tumor-targeting and penetration peptide RGERPPR-modified ferritin
had great potential in enhancing tumor therapy and could be a promising
therapeutic agent.
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Ma, Yuanmeng; Dong, Yixin; Li, Xun; Wang, Fei; Zhang, Yu (2021). Tumor-Penetrating Peptide-Functionalized Ferritin
Enhances Antitumor Activity of Paclitaxel. ACS Publications. Collection. https://doi.org/10.1021/acsabm.0c01613
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AUTHORS (5)
YM
Yuanmeng Ma
YD
Yixin Dong
XL
Xun Li
FW
Fei Wang
YZ
Yu Zhang
KEYWORDS
H chain ferritinMMP -2.binding peptideHFtn-mMMP 2-RGE nanoparticlesRGERPPR motiftumor-penetrating peptide RGERPPR motifPTXprotein shelllinker regionHFtn-mMMP 2-RGE3 D tumor spheroid experimentGGGGSlung cancer cellstumor therapyTumor-Penetrating Peptide-Functiona...linker moietiesMMP -2 cleavage sitetargets tumor cellspenetration peptide RGERPPR-modifie...C-terminalBetter penetrabilityNRP