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Definition
AHNP is a rationally designed biologically active peptidomimetic that mimics an anti-Her2/neu monoclonal antibody (Mab)’s antitumor function. AHNP is the smallest antibody fragment, which is derived from the complementarity determining region (CDR) heavy chain 3 (H3) of the anti-Her2/neu antibody rhuMab 4D5 (Herceptin and Trastuzumab).
Characteristics
The epidermal growth factor (EGF) family of tyrosine kinase receptors includes four structurally related members: erbB1 (EGFR, HER1), erbB2 (Her2/neu, p185), erbB3 (HER3), and erbB4 (HER4). ErbB receptors are crucial for mediating cell proliferation, differentiation, and survival. They are glycoproteins composed of an ectodomain, a single transmembrane region, and a cytoplasmic tyrosine kinase domain flanked by noncatalytic regulatory regions. The ectodomain contains four subdomains: L1, S1, L2, and S2, where L and S are acronyms for large and small, respectively. These subdomains are also referred to as...
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References
Berezov A, Zhang HT, Greene MI et al (2001) Disabling erbB receptors with rationally designed exocyclic mimetics of antibodies: structure-function analysis. J Med Chem 44:2565–2574
Drebin JA, Link VC, Stern DF et al (1985) Down-modulation of an oncogene protein product and reversion of the transformed phenotype by monoclonal antibodies. Cell 41:697–706
Masuda K, Richter M, Song X et al (2006) AHNP-streptavidin: a tetrameric bacterially produced antibody surrogate fusion protein against p185her2/neu. Oncogene 14:7740–7746
Park BW, Zhang HT, Wu C et al (2000) Rationally designed anti-Her2/neu peptide mimetic disables P185Her2/neu tyrosine kinases in vitro and in vivo. Nat Biotechnol 18:194–198
Tan M, Lan KH, Yao J et al (2006) Selective inhibition of ErbB2-overexpressing breast cancer in vivo by a novel TAT-based ErbB2-targeting signal transducers and activators of transcription 3-blocking peptide. Cancer Res 66:3764–3772
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Murali, R., Berezov, A., Greene, M.I. (2015). Anti-Her2/Neu Peptide Mimetic. In: Schwab, M. (eds) Encyclopedia of Cancer. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-46875-3_303
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DOI: https://doi.org/10.1007/978-3-662-46875-3_303
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Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-46874-6
Online ISBN: 978-3-662-46875-3
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