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  BCastagnino  NPonassi  RTomati  VNieddu  EStier  GMalacarne  DParodi  S

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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

机译：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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c-Myc is a transcription modulator protooncogene. 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 K(d)s ranging between 1.3 x 10(-6) and 4.8 x 10(-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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《The FASEB Journal》 |2007年第4期|1256-1263|共8页
作者
Bagnasco L; Tortolina L; Biasotti BCastagnino NPonassi RTomati VNieddu EStier GMalacarne DParodi S;
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作者单位

Univ Genoa, Dept Oncol Biol & Genet, I-16132 Genoa, Italy;

Natl Canc Inst, Expt Oncol Lab, IST, Genoa, Italy;

ISO, Genoa, ItalyUniv Genoa, Dept Pharmaceut Sci, Genoa, ItalyEMBL Heidelberg, Struct & Computat Biol Unit, Heidelberg, Germany;

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原文格式 PDF
正文语种英语
中图分类生物化学;
关键词
inhibitors; MYC/MAX DIMERIZATION; CELL-GROWTH; DNA-BINDING; SEQUENCE; MAX; TRANSFORMATION; TRANSCRIPTION; APOPTOSIS;

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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