Contrast Media & Molecular Imaging
Volume 2018 (2018), Article ID 7929617, 11 pages
https://doi.org/10.1155/2018/7929617
Research Article
Construction and Evaluation of the Tumor-Targeting, Cell-Penetrating Multifunctional Molecular Probe iCREKA
PET Center, Nanfang Hospital, Southern Medical University, Guangzhou, Guangdong 510515, China
Correspondence should be addressed to Quan-shi Wang; ten.361@hplsqw
Received 11 August 2017; Revised 24 December 2017; Accepted 5 February 2018; Published 4 March 2018
Academic Editor: James Frost
Copyright © 2018 Li-juan Wang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Linked References
- S. E. Blondelle and R. A. Houghten, “Hemolytic and antimicrobial activities of the twenty-four individual omission analogues of melittin,” Biochemistry, vol. 30, no. 19, pp. 4671–4678, 1991. View at Publisher · View at Google Scholar · View at Scopus
- T. Higashijima, K. Wakamatsu, M. Takemitsu, M. Fujino, T. Nakajima, and T. Miyazawa, “Conformational change of mastoparan from wasp venom on binding with phospholipid membrane,” FEBS Letters, vol. 152, no. 2, pp. 227–230, 1983. View at Publisher · View at Google Scholar · View at Scopus
- G. P. H. Dietz and M. Bähr, “Delivery of bioactive molecules into the cell: The Trojan horse approach,” Molecular and Cellular Neuroscience, vol. 27, no. 2, pp. 85–131, 2004. View at Publisher · View at Google Scholar · View at Scopus
- B. E. Vogel, S. J. Lee, A. Hildebrand et al., “A novel integrin specificity exemplified by binding of the alpha v beta 5 integrin to the basic domain of the HIV Tat protein and vitronectin,” Journal of Cell Biology, vol. 121, no. 2, pp. 461–468, 1993. View at Google Scholar
- S. Fawell, J. Seery, Y. Daikh et al., “Tat-mediated delivery of heterologous proteins into cells,” Proceedings of the National Acadamy of Sciences of the United States of America, vol. 91, no. 2, pp. 664–668, 1994. View at Publisher · View at Google Scholar · View at Scopus
- H. Brooks, B. Lebleu, and E. Vivès, “Tat peptide-mediated cellular delivery: back to basics,” Advanced Drug Delivery Reviews, vol. 57, no. 4, pp. 559–577, 2005. View at Publisher · View at Google Scholar · View at Scopus
- F. Said Hassane, A. F. Saleh, R. Abes, M. J. Gait, and B. Lebleu, “Cell penetrating peptides: overview and applications to the delivery of oligonucleotides,” Cellular and Molecular Life Sciences, vol. 67, no. 5, pp. 715–726, 2010. View at Publisher · View at Google Scholar · View at Scopus
- J. P. Richard, K. Melikov, E. Vives et al., “Cell-penetrating peptides: A reevaluation of the mechanism of cellular uptake,” The Journal of Biological Chemistry, vol. 278, no. 1, pp. 585–590, 2003. View at Publisher · View at Google Scholar · View at Scopus
- C. Palm-Apergi, A. Lorents, K. Padari, M. Pooga, and M. Hällbrink, “The membrane repair response masks membrane disturbances caused by cell-penetrating peptide uptake,” The FASEB Journal, vol. 23, no. 1, pp. 214–223, 2009. View at Publisher · View at Google Scholar · View at Scopus
- I. Mäger, E. Eiríksdóttir, K. Langel, S. EL Andaloussi, and Ü. Langel, “Assessing the uptake kinetics and internalization mechanisms of cell-penetrating peptides using a quenched fluorescence assay,” Biochimica et Biophysica Acta, vol. 1798, no. 3, pp. 338–343, 2010. View at Publisher · View at Google Scholar · View at Scopus
- A. D. Frankel and C. O. Pabo, “Cellular uptake of the tat protein from human immunodeficiency virus,” Cell, vol. 55, no. 6, pp. 1189–1193, 1988. View at Publisher · View at Google Scholar · View at Scopus
- M. Rusnati, D. Coltrini, P. Oreste et al., “Interaction of HIV-1 Tat protein with heparin. Role of the backbone structure, sulfation, and size,” The Journal of Biological Chemistry, vol. 272, no. 17, pp. 11313–11320, 1997. View at Publisher · View at Google Scholar · View at Scopus
- A. Prochiantz, “Messenger proteins: homeoproteins, TAT and others,” Current Opinion in Cell Biology, vol. 12, no. 4, pp. 400–406, 2000. View at Publisher · View at Google Scholar · View at Scopus
- L. Roth, L. Agemy, V. R. Kotamraju et al., “Transtumoral targeting enabled by a novel neuropilin-binding peptide,” Oncogene, vol. 31, no. 33, pp. 3754–3763, 2012. View at Publisher · View at Google Scholar · View at Scopus
- P. Laakkonen, K. Porkka, J. A. Hoffman, and E. Ruoslahti, “A tumor-homing peptide with a targeting specificity related to lymphatic vessels,” Nature Medicine, vol. 8, no. 7, pp. 751–755, 2002. View at Publisher · View at Google Scholar · View at Scopus
- P. Laakkonen, M. E. Åkerman, H. Biliran et al., “Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells,” Proceedings of the National Acadamy of Sciences of the United States of America, vol. 101, no. 25, pp. 9381–9386, 2004. View at Publisher · View at Google Scholar · View at Scopus
- V. Fogal, L. Zhang, S. Krajewski, and E. Ruoslahti, “Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma,” Cancer Research, vol. 68, no. 17, pp. 7210–7218, 2008. View at Publisher · View at Google Scholar · View at Scopus
- J. Park, G. von Maltzahn, M. J. Xu et al., “Cooperative nanomaterial system to sensitize, target, and treat tumors,” Proceedings of the National Acadamy of Sciences of the United States of America, vol. 107, no. 3, pp. 981–986, 2010. View at Publisher · View at Google Scholar
- T. P. Herringson and J. G. Altin, “Effective tumor targeting and enhanced anti-tumor effect of liposomes engrafted with peptides specific for tumor lymphatics and vasculature,” International Journal of Pharmaceutics, vol. 411, no. 1-2, pp. 206–214, 2011. View at Publisher · View at Google Scholar · View at Scopus
- F. Zhang, G. Niu, X. Lin et al., “Imaging tumor-induced sentinel lymph node lymphangiogenesis with LyP-1 peptide,” Amino Acids, vol. 42, no. 6, pp. 2343–2351, 2012. View at Publisher · View at Google Scholar · View at Scopus
- R. B. Merrifield, “Solid-phase peptide synthesis. III. An improved synthesis of bradykinin,” Biochemistry, vol. 3, no. 9, pp. 1385–1390, 1964. View at Publisher · View at Google Scholar · View at Scopus
- F. T. Chin, B. Shen, S. Liu et al., “First experience with clinical-grade [18F]FPP (RGD) 2: An automated multi-step radiosynthesis for clinical PET studies,” Molecular Imaging and Biology, vol. 14, no. 1, pp. 88–95, 2012. View at Publisher · View at Google Scholar · View at Scopus
- T. Wehner, “The role of functional imaging in the tumor patient,” Epilepsia, vol. 54, no. 9, pp. 44–49, 2013. View at Publisher · View at Google Scholar · View at Scopus
- C. Viswanathan, P. R. Bhosale, S. N. Shah, and R. Vikram, “Positron Emission Tomography-Computed Tomography Imaging for Malignancies in Women,” Radiologic Clinics of North America, vol. 51, no. 6, pp. 1111–1125, 2013. View at Publisher · View at Google Scholar · View at Scopus
- H. Jadvar, “Molecular imaging of prostate cancer with PET,” Journal of Nuclear Medicine, vol. 54, no. 10, pp. 1685–1688, 2013. View at Publisher · View at Google Scholar · View at Scopus
- S. Mirpour, J. C. Mhlanga, P. Logeswaran, G. Russo, G. Mercier, and R. M. Subramaniam, “The role of PET/CT in the management of cervical cancer,” American Journal of Roentgenology, vol. 201, no. 2, pp. W192–W205, 2013. View at Publisher · View at Google Scholar · View at Scopus
- B. Bai, J. Bading, and P. S. Conti, “Tumor quantification in clinical positron emission tomography,” Theranostics, vol. 3, no. 10, pp. 787–801, 2013. View at Publisher · View at Google Scholar · View at Scopus
- H. Hoshikawa, T. Mori, Y. Yamamoto et al., “Prognostic value comparison between 18F-FLT PET/CT and 18F-FDG PET/CT volume-based metabolic parameters in patients with head and neck cancer,” Clinical Nuclear Medicine, vol. 40, no. 6, pp. 464–468, 2015. View at Publisher · View at Google Scholar · View at Scopus
- S. Kwee, L. Wong, B. Hernandez, O. Chan, M. Sato, and N. Tsai, “Chronic liver disease and the detection of hepatocellular carcinoma by [18F]fluorocholine PET/CT,” Diagnostics, vol. 5, no. 4, pp. 189–199, 2015. View at Publisher · View at Google Scholar
- M. Bieze, H.-J. Klümpen, J. Verheij et al., “Diagnostic accuracy of 18F-methylcholine positron emission tomography/computed tomography for intra- and extrahepatic hepatocellular carcinoma,” Hepatology, vol. 59, no. 3, pp. 996–1006, 2014. View at Publisher · View at Google Scholar · View at Scopus
- D. Simberg, T. Duza, J. H. Park et al., “Biomimetic amplification of nanoparticle homing to tumors,” Proceedings of the National Acadamy of Sciences of the United States of America, vol. 104, no. 3, pp. 932–936, 2007. View at Publisher · View at Google Scholar · View at Scopus
- J. Pilch, D. M. Brown, M. Komatsu et al., “Peptides selected for binding to clotted plasma accumulate in tumor stroma and wounds,” Proceedings of the National Acadamy of Sciences of the United States of America, vol. 103, no. 8, pp. 2800–2804, 2006. View at Publisher · View at Google Scholar · View at Scopus
- M. Libra, A. Scalisi, N. Vella et al., “Uterine cervical carcinoma: role of matrix metalloproteinases (review),” International Journal of Oncology, vol. 34, no. 4, pp. 897–903, 2009. View at Publisher · View at Google Scholar · View at Scopus
- A. Ghosh, A. Moirangthem, R. Dalui et al., “Expression of matrix metalloproteinase-2 and 9 in cervical intraepithelial neoplasia and cervical carcinoma among different age groups of premenopausal and postmenopausal women,” Journal of Cancer Research and Clinical Oncology, vol. 140, no. 9, pp. 1585–1593, 2014. View at Publisher · View at Google Scholar · View at Scopus
- B. Davies, J. Waxman, H. Wasan et al., “Levels of Matrix Metalloproteases in Bladder Cancer Correlate with Tumor Grade and Invasion,” Cancer Research, vol. 53, no. 22, pp. 5365–5369, 1993. View at Google Scholar · View at Scopus
- M. H. Tayebjee, G. Y. H. Lip, and R. J. MacFadyen, “Matrix metalloproteinases in coronary artery disease: Clinical and therapeutic implications and pathological significance,” Current Medicinal Chemistry, vol. 12, no. 8, pp. 917–925, 2005. View at Publisher · View at Google Scholar · View at Scopus
- A. G. Arroyo, L. Genís, P. Gonzalo, S. Matías-Román, A. Pollán, and B. G. Gálvez, “Matrix metalloproteinases: New routes to the use of MT1-MMP as a therapeutic target in angiogenesis-related disease,” Current Pharmaceutical Design, vol. 13, no. 17, pp. 1787–1802, 2007. View at Publisher · View at Google Scholar · View at Scopus
- H. J. Breyholz, S. Wagner, B. Levkau et al., “A 18F-radiolabeled analogue of CGS 27023A as a potential agent for assessment of matrix-metalloproteinase activity in vivo,” The Quarterly Journal of Nuclear Medicine and Molecular Imaging, vol. 51, no. 1, pp. 24–32, 2007. View at Google Scholar
- D. Zanuy, F. J. Sayago, G. Revilla-López et al., “Engineering strategy to improve peptide analogs: From structure-based computational design to tumor homing,” Journal of Computer-Aided Molecular Design, vol. 27, no. 1, pp. 31–43, 2013. View at Publisher · View at Google Scholar · View at Scopus