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Identification of a targeting‐delivery peptide based on rhCNB
Author(s) -
Yang Jinju,
Gao Yadan,
Zhu Ziwei,
Qin Nannan,
Wei Qun
Publication year - 2019
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3159
Subject(s) - internalization , recombinant dna , calcineurin , protein subunit , immunoprecipitation , chemistry , cancer research , microbiology and biotechnology , peptide , receptor , biology , transplantation , biochemistry , medicine , gene , surgery
Calcineurin B subunit (CNB) is the regulatory subunit of calcineurin (CN), and its classical function is to regulate the activity of CN. Research in our laboratory has revealed that the recombinant human CNB (rhCNB) is a good antitumor candidate and can be internalized by tumor cells via TLR4 receptor complexes and targeted to tumor tissue in nude mice. However, the fragment or domain of rhCNB mediating internalization and target delivery has not been identified. To explore fragment‐ mediated rhCNB internalization and target delivery, we generated truncated derivatives of rhCNBs by recombinant DNA technology and examined their cellular uptake. Interactions between truncated rhCNBs and the TLR4 receptor were studied by ELISA and co‐immunoprecipitation, and targeting of model tumors in nude mice was examined. The results showed that one truncated derivative, Trun3 (124‐169aa), was taken up by cells and targeted tumors with almost the same efficiency as intact rhCNB. These results indicate that Trun3 (45aa) contains the major sequence responsible for rhCNB internalization and tumor targeting and might be developed for drug delivery to tumors.