Urokinase-controlled tumor penetrating peptide
Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identifie...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Braun, Gary B. [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2016transfer abstract |
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| Umfang: |
8 |
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| Übergeordnetes Werk: |
Enthalten in: 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up - Moschini, M. ELSEVIER, 2015, official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems, New York, NY [u.a.] |
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| Übergeordnetes Werk: |
volume:232 ; year:2016 ; day:28 ; month:06 ; pages:188-195 ; extent:8 |
| Links: |
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| DOI / URN: |
10.1016/j.jconrel.2016.04.027 |
|---|
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| 520 | |a Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. | ||
| 520 | |a Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. | ||
| 700 | 1 | |a Sugahara, Kazuki N. |4 oth | |
| 700 | 1 | |a Yu, Olivia M. |4 oth | |
| 700 | 1 | |a Kotamraju, Venkata Ramana |4 oth | |
| 700 | 1 | |a Mölder, Tarmo |4 oth | |
| 700 | 1 | |a Lowy, Andrew M. |4 oth | |
| 700 | 1 | |a Ruoslahti, Erkki |4 oth | |
| 700 | 1 | |a Teesalu, Tambet |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a Moschini, M. ELSEVIER |t 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up |d 2015 |d official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems |g New York, NY [u.a.] |w (DE-627)ELV012920894 |
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2016 |
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10.1016/j.jconrel.2016.04.027 doi GBVA2016005000008.pica (DE-627)ELV03511908X (ELSEVIER)S0168-3659(16)30240-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 610 VZ 670 VZ 35.80 bkl Braun, Gary B. verfasserin aut Urokinase-controlled tumor penetrating peptide 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Sugahara, Kazuki N. oth Yu, Olivia M. oth Kotamraju, Venkata Ramana oth Mölder, Tarmo oth Lowy, Andrew M. oth Ruoslahti, Erkki oth Teesalu, Tambet oth Enthalten in Elsevier Moschini, M. ELSEVIER 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up 2015 official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems New York, NY [u.a.] (DE-627)ELV012920894 volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 https://doi.org/10.1016/j.jconrel.2016.04.027 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_22 GBV_ILN_40 GBV_ILN_105 35.80 Makromolekulare Chemie VZ AR 232 2016 28 0628 188-195 8 045F 540 |
| spelling |
10.1016/j.jconrel.2016.04.027 doi GBVA2016005000008.pica (DE-627)ELV03511908X (ELSEVIER)S0168-3659(16)30240-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 610 VZ 670 VZ 35.80 bkl Braun, Gary B. verfasserin aut Urokinase-controlled tumor penetrating peptide 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Sugahara, Kazuki N. oth Yu, Olivia M. oth Kotamraju, Venkata Ramana oth Mölder, Tarmo oth Lowy, Andrew M. oth Ruoslahti, Erkki oth Teesalu, Tambet oth Enthalten in Elsevier Moschini, M. ELSEVIER 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up 2015 official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems New York, NY [u.a.] (DE-627)ELV012920894 volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 https://doi.org/10.1016/j.jconrel.2016.04.027 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_22 GBV_ILN_40 GBV_ILN_105 35.80 Makromolekulare Chemie VZ AR 232 2016 28 0628 188-195 8 045F 540 |
| allfields_unstemmed |
10.1016/j.jconrel.2016.04.027 doi GBVA2016005000008.pica (DE-627)ELV03511908X (ELSEVIER)S0168-3659(16)30240-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 610 VZ 670 VZ 35.80 bkl Braun, Gary B. verfasserin aut Urokinase-controlled tumor penetrating peptide 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Sugahara, Kazuki N. oth Yu, Olivia M. oth Kotamraju, Venkata Ramana oth Mölder, Tarmo oth Lowy, Andrew M. oth Ruoslahti, Erkki oth Teesalu, Tambet oth Enthalten in Elsevier Moschini, M. ELSEVIER 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up 2015 official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems New York, NY [u.a.] (DE-627)ELV012920894 volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 https://doi.org/10.1016/j.jconrel.2016.04.027 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_22 GBV_ILN_40 GBV_ILN_105 35.80 Makromolekulare Chemie VZ AR 232 2016 28 0628 188-195 8 045F 540 |
| allfieldsGer |
10.1016/j.jconrel.2016.04.027 doi GBVA2016005000008.pica (DE-627)ELV03511908X (ELSEVIER)S0168-3659(16)30240-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 610 VZ 670 VZ 35.80 bkl Braun, Gary B. verfasserin aut Urokinase-controlled tumor penetrating peptide 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Sugahara, Kazuki N. oth Yu, Olivia M. oth Kotamraju, Venkata Ramana oth Mölder, Tarmo oth Lowy, Andrew M. oth Ruoslahti, Erkki oth Teesalu, Tambet oth Enthalten in Elsevier Moschini, M. ELSEVIER 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up 2015 official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems New York, NY [u.a.] (DE-627)ELV012920894 volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 https://doi.org/10.1016/j.jconrel.2016.04.027 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_22 GBV_ILN_40 GBV_ILN_105 35.80 Makromolekulare Chemie VZ AR 232 2016 28 0628 188-195 8 045F 540 |
| allfieldsSound |
10.1016/j.jconrel.2016.04.027 doi GBVA2016005000008.pica (DE-627)ELV03511908X (ELSEVIER)S0168-3659(16)30240-1 DE-627 ger DE-627 rakwb eng 540 610 540 DE-600 610 DE-600 610 VZ 670 VZ 35.80 bkl Braun, Gary B. verfasserin aut Urokinase-controlled tumor penetrating peptide 2016transfer abstract 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. Sugahara, Kazuki N. oth Yu, Olivia M. oth Kotamraju, Venkata Ramana oth Mölder, Tarmo oth Lowy, Andrew M. oth Ruoslahti, Erkki oth Teesalu, Tambet oth Enthalten in Elsevier Moschini, M. ELSEVIER 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up 2015 official journal of the Controlled Release Society and of the Japanese Society of Drug Delivery Systems New York, NY [u.a.] (DE-627)ELV012920894 volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 https://doi.org/10.1016/j.jconrel.2016.04.027 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U GBV_ILN_22 GBV_ILN_40 GBV_ILN_105 35.80 Makromolekulare Chemie VZ AR 232 2016 28 0628 188-195 8 045F 540 |
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Enthalten in 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up New York, NY [u.a.] volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 |
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Enthalten in 537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up New York, NY [u.a.] volume:232 year:2016 day:28 month:06 pages:188-195 extent:8 |
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537 Early, intermediate and late recurrence after radical cystectomy due to bladder cancer: The necessity of a tailored follow up |
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Braun, Gary B. @@aut@@ Sugahara, Kazuki N. @@oth@@ Yu, Olivia M. @@oth@@ Kotamraju, Venkata Ramana @@oth@@ Mölder, Tarmo @@oth@@ Lowy, Andrew M. @@oth@@ Ruoslahti, Erkki @@oth@@ Teesalu, Tambet @@oth@@ |
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urokinase-controlled tumor penetrating peptide |
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Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. |
| abstractGer |
Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. |
| abstract_unstemmed |
Tumor penetrating peptides contain a cryptic (R/K)XX(R/K) CendR element that must be C-terminally exposed to trigger neuropilin-1 (NRP-1) binding, cellular internalization and malignant tissue penetration. The specific proteases that are involved in processing of tumor penetrating peptides identified using phage display are not known. Here we design de novo a tumor-penetrating peptide based on consensus cleavage motif of urokinase-type plasminogen activator (uPA). We expressed the peptide, uCendR (RPARSGR↓SAGGSVA, ↓ shows cleavage site), on phage or coated it onto silver nanoparticles and showed that it is cleaved by uPA, and that the cleavage triggers binding to recombinant NRP-1 and to NPR-1-expressing cells. Upon systemic administration to mice bearing uPA-overexpressing breast tumors, FAM-labeled uCendR peptide and uCendR-coated nanoparticles preferentially accumulated in tumor tissue. We also show that uCendR phage internalization into cultured cancer cells and its penetration in explants of murine tumors and clinical tumor explants can be potentiated by combining the uCendR peptide with tumor-homing module, CRGDC. |
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Sugahara, Kazuki N. Yu, Olivia M. Kotamraju, Venkata Ramana Mölder, Tarmo Lowy, Andrew M. Ruoslahti, Erkki Teesalu, Tambet |
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