Please use this identifier to cite or link to this item: https://doi.org/10.1186/1756-9966-28-59
Title: Development of a novel small antibody that retains specificity for tumor targeting
Authors: Zhen, Z.-P
Zhang, J 
Zhang, S.-Y
Keywords: antineoplastic agent
immunoglobulin F(ab) fragment
monoclonal antibody
monoclonal antibody colicin Ia
protomimecin
single chain fragment variable antibody
unclassified drug
antibody
hybrid protein
animal cell
animal cell culture
animal experiment
animal model
animal tissue
antigen specificity
article
breast cancer
cancer inhibition
carboxy terminal sequence
cell strain MCF 7
controlled study
drug cytotoxicity
drug distribution
drug protein binding
female
human
human cell
human cell culture
in vitro study
in vivo study
mouse
nonhuman
priority journal
tumor volume
animal
antibody specificity
cell line
cell survival
drug screening
gene vector
genetics
immunology
metabolism
neoplasm
nude mouse
pathology
sensitivity and specificity
Animals
Antibodies
Antibody Specificity
Cell Line
Cell Survival
Female
Genetic Vectors
Humans
Mice
Mice, Nude
Neoplasms
Recombinant Fusion Proteins
Sensitivity and Specificity
Xenograft Model Antitumor Assays
Issue Date: 2009
Publisher: BMC
Citation: Zhen, Z.-P, Zhang, J, Zhang, S.-Y (2009). Development of a novel small antibody that retains specificity for tumor targeting. Journal of Experimental and Clinical Cancer Research 28 (1) : 59. ScholarBank@NUS Repository. https://doi.org/10.1186/1756-9966-28-59
Rights: Attribution 4.0 International
Abstract: Background. For the targeted therapy of solid tumor mediated by monoclonal antibody (mAb), there have different models of rebuilding small antibodies originated from native ones. Almost all natural antibody molecules have the similar structure and conformation, but those rebuilt small antibodies cannot completely keep the original traits of parental antibodies, especially the reduced specificity, which gravely influences the efficacy of small antibodies. Methods. In this study, authors developed a novel mimetic in the form of V HFRIc-10-VHCDRI-VHFR2-V LCDR3-VLFR4N-10 for a parental mAb induced with human breast cancer, and the mimetic moiety was conjugated to the C-terminal of toxicin colicin Ia. The novel fusion peptide, named protomimecin (PMN), was administered to MCF-7 breast cancer cells to demonstrate its killing competency in vitro and in vivo. Results. Compared with original antibody-colicin Ia (Fab-Ia) and single-chain antibody-colicin Ia (Sc-Ia) fusion proteins, PMN retained the targeting specificity of parental antibody and could specifically kill MCF-7 cells in vitro. By injecting intraperitoneally into BALB/c athymic mice bearing MCF-7 tumors, with reduced affinity, PMN significantly suppressed the growth of tumors compared with control mice treated by toxicin protein, Fab-Ia protein, Sc-Ia protein or by PBS (p < 0.05). Conclusion. This novel mimetic antibody retained original specificity of parental antibody, and could effectively guide killer moiety to suppress the growth of breast cancer by targeted cell death. © 2009 Zhen et al.
Source Title: Journal of Experimental and Clinical Cancer Research
URI: https://scholarbank.nus.edu.sg/handle/10635/178220
ISSN: 1756-9966
DOI: 10.1186/1756-9966-28-59
Rights: Attribution 4.0 International
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