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  Inhibition of a protein-protein interaction between INI1 and c-Myc by small peptidomimetic molecules inspired by Helix-1 of c-Myc: identification of a new target of potential antineoplastic interest

Bagnasco, L., Tortolina, L., Biasotti, B., Castagnino, N., Ponassi, R., Tomati, V., et al. (2007). Inhibition of a protein-protein interaction between INI1 and c-Myc by small peptidomimetic molecules inspired by Helix-1 of c-Myc: identification of a new target of potential antineoplastic interest. The FASEB Journal, 21(4), 1256-1263. doi:10.1096/fj.06-7082com.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-AB9A-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-AB9B-B
Genre: Journal Article
Alternative Title : Inhibition of a protein-protein interaction between INI1 and c-Myc by small peptidomimetic molecules inspired by Helix-1 of c-Myc: identification of a new target of potential antineoplastic interest

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Bagnasco, L., Author
Tortolina, L., Author
Biasotti, B., Author
Castagnino, N., Author
Ponassi, R., Author
Tomati, V., Author
Nieddu, E., Author
Stier, Gunter1, Author              
Malacarne, D., Author
Parodi, S., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: inhibitors
 Abstract: c-Myc is a transcription modulator proto-oncogene. When overexpressed, it becomes an important contributor to the multi-hit process of malignant transformation. In two earlier papers in this journal (see refs. 19 , 20) we reported that retro-inverso peptidomimetic molecules inspired by the Helix-1 of c-Myc motif could be sequence-specific antiproliferative agents active in the low micromolar range. We also found that our peptides were not opening the four-alpha-helix Myc:Max bundle. Their antiproliferative activity in cancer cell lines needs the presence of side chains projecting outside of the bundle in the corresponding native H1 motif. This observation suggested interference with an external partner. In this study we investigated the INI1:Myc interaction. INI1 is a subunit of the SWI/SNF complex (component of the enhanceosome surrounding Myc:Max heterodimer). The INI1:Myc interaction was confirmed via pull down, ELISA, and fluorescence anisotropy assays. According to the length of INI1 fragments used, we calculated Kds ranging between 1.3x10(-6) and 4.8x10(-7) M. The three different techniques applied showed that the INI1:Myc interaction was also the target of our retro-inverso peptidomimetic molecules, which seem to bind specifically at INI1. A Myc binding, 21aa INI1 fragment (minimum interacting sequence), could inspire the synthesis of a new class of more selective c-Myc inhibitors.

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Language(s): eng - English
 Dates: 2006-08-182006-11-092007-01-102007-04-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: The FASEB Journal
  Other : FASEB J.
Source Genre: Journal
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Publ. Info: Bethesda, Md. : The Federation
Pages: - Volume / Issue: 21 (4) Sequence Number: - Start / End Page: 1256 - 1263 Identifier: ISSN: 0892-6638
CoNE: https://pure.mpg.de/cone/journals/resource/954927535970_1