alexa Tumor-penetrating Peptide Fused EGFR Single-domain Antibody Enhances Cancer Drug Penetration Into 3D Multicellular Spheroids And Facilitates Effective Gastric Cancer Therapy
ISSN: 2329-6887

Journal of Pharmacovigilance
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9th International Conference and Exhibition on Pharmacovigilance & Drug Safety
July 17-18, 2017 Munich, Germany

Huizi Sha
Comprehensive Cancer Center of Drum-Tower Hospital, China
Medical School of Nanjing University, China
Posters & Accepted Abstracts: J Pharmacovigil
DOI: 10.4172/2329-6887-C1-027
Abstract
Human tumors, including gastric cancer, frequently express high levels of epidermal growth factor receptors (EGFRs), which are associated with a poor prognosis. Targeted delivery of anticancer drugs to cancerous tissues shows potential in sparing unaffected tissues. However, it has been a major challenge for drug penetration in solid tumor tissues due to the complicated tumor microenvironment. We have constructed a recombinant protein named anti-EGFR-iRGD consisting of an anti-EGFR VHH (the variable domain from the heavy chain of the antibody) fused to iRGD, a tumor-specific binding peptide with high permeability. Anti- EGFR-iRGD, which targets EGFR and αvβ3, spreads extensively throughout both the multicellular spheroids and the tumor mass. The recombinant protein anti-EGFR-iRGD also exhibited antitumor activity in tumor cell lines, multicellular spheroids, and mice. Moreover, anti-EGFR-iRGD could improve anticancer drugs, such as doxorubicin (DOX), bevacizumab, nanoparticle permeability and efficacy in multicellular spheroids. This study draws attention to the importance of iRGD peptide in the therapeutic approach of anti-EGFR-iRGD. As a consequence, anti-EGFR-iRGD could be a drug candidate for cancer treatment and a useful adjunct of other anticancer drugs.
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