Characterization of a specific phage-displayed peptide binding to vasculature of human gastric cancer

Mao, Zhi; Wu, Kaichun; Dong, Lei; Hao, Zhiming; Deng, Tao-Zhi; Liu, Hong; Liang, Shuhui; Zhao, Peng; Qiao, Tiankui; Yu, Wenbin; Xu, Xingguang; Fan, Daiming

doi:10.4161/cbt.3.12.1223

Cited by 58 publications

(28 citation statements)

References 15 publications

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“…40 whereas the binding effect of GX1 peptide with cultured HepG2 cells was not significant. 41 Furthermore, according to the results, it was found that the targeting effects of the corresponding NPs to hepatocellular carcinoma were slightly better than lung cancer. A further comparison indicated that a lower but not negligible cytotoxic effect has also been observed on normal hepatocytes.…”

Section: In Vitro Cytotoxicitymentioning

confidence: 95%

“…This high accumulation of NPs in HepG2 cells enhanced the intracellular release of DOX. 41,47 Correspondingly, the apoptosis of HepG2 cells induced by DOX-loaded RGD-GX1-modified NPs was more effective than free DOX.…”

Section: Exploration Of the Fas-mediated Apoptotic Mechanismmentioning

confidence: 99%

“…42 In addition, a weak binding of GX1 to HepG2 cells was also observed in specific phage-displayed peptide binding experiment by Zhi et al, although GX1 mainly selectively targeted to vascular endothelium of tumor. 41 Therefore, there was more or less synergistic effect of the targeting to HepG2 cells in vitro through the mediation of RGD-GX1 heterogeneous dimer peptide. This high accumulation of NPs in HepG2 cells enhanced the intracellular release of DOX.…”

Section: Exploration Of the Fas-mediated Apoptotic Mechanismmentioning

confidence: 99%

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Heterogeneous dimer peptide-conjugated polylysine dendrimer-Fe3O4 composite as a novel nanoscale molecular probe for early diagnosis and therapy in hepatocellular carcinoma

Shen¹,

Li²,

Fan³

et al. 2017

IJN

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A novel nanoscale molecular probe is formulated in order to reduce toxicity and side effects of antitumor drug doxorubicin (DOX) in normal tissues and to enhance the detection sensitivity during early imaging diagnosis. The mechanism involves a specific targeting of Arg-Gly-Asp peptide (RGD)-GX1 heterogeneous dimer peptide-conjugated dendrigraft poly- l -lysine (DGL)–magnetic nanoparticle (MNP) composite by α v β 3 -integrin/vasculature endothelium receptor-mediated synergetic effect. The physicochemical properties of the nanoprobe were characterized by using transmission electron microscope, Fourier transform infrared spectroscopy, X-ray diffraction, dynamic light scattering (DLS), and vibrating sample magnetometer. The average diameter of the resulting MNP–DGL–RGD-GX1–DOX nanoparticles (NPs) was ~150−160 nm by DLS under simulate physiological medium. In the present experimental system, the loading amount of DOX on NPs accounted for 414.4 mg/g for MNP–DGL–RGD-GX1–DOX. The results of cytotoxicity, flow cytometry, and cellular uptake consistently indicated that the MNP–DGL–RGD-GX1–DOX NPs were inclined to target HepG2 cells in selected three kinds of cells. In vitro exploration of molecular mechanism revealed that cell apoptosis was associated with the overexpression of Fas protein and the significant activation of caspase-3. In vivo magnetic resonance imaging and biodistribution study showed that the MNP–DGL–RGD-GX1–DOX formulation had high affinity to the tumor tissue, leading to more aggregation of NPs in the tumor. In vivo antitumor efficacy research verified that MNP–DGL–RGD-GX1–DOX NPs possessed significant antitumor activity and the tumor inhibitory rate reached 78.5%. These results suggested that NPs could be promising in application to early diagnosis and therapy in hepatocellular carcinoma as a specific nanoprobe.

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Section: In Vitro Cytotoxicitymentioning

confidence: 95%

Section: Exploration Of the Fas-mediated Apoptotic Mechanismmentioning

confidence: 99%

Section: Exploration Of the Fas-mediated Apoptotic Mechanismmentioning

confidence: 99%

See 1 more Smart Citation

Heterogeneous dimer peptide-conjugated polylysine dendrimer-Fe3O4 composite as a novel nanoscale molecular probe for early diagnosis and therapy in hepatocellular carcinoma

Shen¹,

Li²,

Fan³

et al. 2017

IJN

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“…GX1 was identified by Min Zhi et al in 2004 by screening a phage-displayed peptide library in vivo [5] and was appraised and further studied by Xiaoli Hui et al [6][7][8][9][10]. Previous results indicated that GX1 was able to bind specifically to the tumor vasculature and could be applied to anti-angiogenesis iatreusis of cancer, together with anti-neoplastic agents, as a novel tumor vascular marker.…”

Section: Introductionmentioning

confidence: 96%

Evaluation of Tc-99 m Labeled Dimeric GX1 Peptides for Imaging of Colorectal Cancer Vasculature

et al. 2015

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“…Immunohistochemistry staining in mouse and human tissue showed that this phage peptide could specifically bind to the endothelial cells of human gastric cancer [5]. We have also labeled GX1 with 99 Tc m O 4 -for in vivo dynamic imaging of tumor xenografts using SPECT, and the results provided an imaging evidence for gastric cancer angiogenesis-targeted radiotherapy as well as other therapeutic strategies based on specific vascular markers [6].…”

Section: Introductionmentioning

confidence: 97%

Expression, Purification, and Characterization of Recombinant Protein GX1-rmhTNFα

Cao

Liu

et al. 2009

Mol Biotechnol

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A phage-displayed peptide CGNSNPKSC (GX1) was obtained previously in our lab, which could specifically bind to the vasculature of human gastric cancer. GX1-rmhTNFalpha was a fusion protein of GX1 and recombinant mutant human tumor necrosis factor alpha (rmhTNFalpha), which was designed by us with the expectation of enhancing selectivity of rmhTNFalpha. The DNA fragment encoding GX1 was cloned into the vector pBV220 with rmhTNFalpha between the EcoRI site and the BamHI site, and then expressed in Escherichia coli DH5alpha by temperature induction. Subsequently, E. coli DH5alpha was lysed, and the GX1-rmhTNFalpha protein was found in both soluble form and inclusion bodies. The protein was fractionated with ammonium sulfate deposition from 30% to 60%, and purified by cation and anion exchange chromatography using SP Sepharose Fast Flow column and Q Sepharose Fast Flow column. The purity of protein was then identified by SDS-PAGE and HPLC. Subsequent studies showed that GX1-rmhTNFalpha had high bioactivity of 5.65 x 10(8) IU/ml, which was similar with natural human TNFalpha and could reach the tumor site relatively faster than rmhTNFalpha.

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Characterization of a specific phage-displayed peptide binding to vasculature of human gastric cancer

Cited by 58 publications

References 15 publications

Heterogeneous dimer peptide-conjugated polylysine dendrimer-Fe<sub>3</sub>O<sub>4 </sub>composite as a novel nanoscale molecular probe for early diagnosis and therapy in hepatocellular carcinoma

Heterogeneous dimer peptide-conjugated polylysine dendrimer-Fe<sub>3</sub>O<sub>4 </sub>composite as a novel nanoscale molecular probe for early diagnosis and therapy in hepatocellular carcinoma

Evaluation of Tc-99 m Labeled Dimeric GX1 Peptides for Imaging of Colorectal Cancer Vasculature

Expression, Purification, and Characterization of Recombinant Protein GX1-rmhTNFα

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