New Phage Display-Isolated Heptapeptide Recognizing the Regulatory Carboxy-Terminal Domain of Human Tumour Protein p53.
Identifieur interne : 000399 ( Main/Exploration ); précédent : 000398; suivant : 000400New Phage Display-Isolated Heptapeptide Recognizing the Regulatory Carboxy-Terminal Domain of Human Tumour Protein p53.
Auteurs : Sihem Ben Abid [Tunisie] ; Mouna Sahnoun [Tunisie] ; Ines Yacoubi-Hadj Amor [Tunisie] ; Salma Abdelmoula-Souissi [Tunisie] ; Hajer Hassairi [Tunisie] ; Raja Mokdad-Gargouri [Tunisie] ; Ali Gargouri [Tunisie]Source :
- The protein journal [ 1875-8355 ] ; 2017.
Descripteurs français
- KwdFr :
- Apoptose (MeSH), Banque de peptides (MeSH), Biotine (métabolisme), Escherichia coli (génétique), Fluorescéine-5-isothiocyanate (métabolisme), Glutathione transferase (génétique), Humains (MeSH), Peptides (composition chimique), Peptides (génétique), Peptides (métabolisme), Protéine p53 suppresseur de tumeur (composition chimique), Protéine p53 suppresseur de tumeur (génétique), Protéine p53 suppresseur de tumeur (métabolisme), Protéines de fusion recombinantes (composition chimique), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Simulation de docking moléculaire (MeSH).
- MESH :
- composition chimique : Peptides, Protéine p53 suppresseur de tumeur, Protéines de fusion recombinantes.
- génétique : Escherichia coli, Glutathione transferase, Peptides, Protéine p53 suppresseur de tumeur, Protéines de fusion recombinantes.
- métabolisme : Biotine, Fluorescéine-5-isothiocyanate, Peptides, Protéine p53 suppresseur de tumeur, Protéines de fusion recombinantes.
- Apoptose, Banque de peptides, Humains, Simulation de docking moléculaire.
English descriptors
- KwdEn :
- Apoptosis (MeSH), Biotin (metabolism), Escherichia coli (genetics), Fluorescein-5-isothiocyanate (metabolism), Glutathione Transferase (genetics), Humans (MeSH), Molecular Docking Simulation (MeSH), Peptide Library (MeSH), Peptides (chemistry), Peptides (genetics), Peptides (metabolism), Recombinant Fusion Proteins (chemistry), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Tumor Suppressor Protein p53 (chemistry), Tumor Suppressor Protein p53 (genetics), Tumor Suppressor Protein p53 (metabolism).
- MESH :
- chemical , chemistry : Peptides, Recombinant Fusion Proteins, Tumor Suppressor Protein p53.
- chemical , genetics : Glutathione Transferase, Peptides, Recombinant Fusion Proteins, Tumor Suppressor Protein p53.
- chemical , metabolism : Biotin, Fluorescein-5-isothiocyanate, Peptides, Recombinant Fusion Proteins, Tumor Suppressor Protein p53.
- genetics : Escherichia coli.
- Apoptosis, Humans, Molecular Docking Simulation, Peptide Library.
Abstract
The transcription factor tumor protein p53 (P53) controls a variety of genes most involved in cell cycle and is at the origin of apoptosis when DNA is irreparably damaged. We planned to select novel tumor protein p53-interacting peptides through the screening of hepta-peptide phage-display libraries. For this aim, human tumor suppressor protein p53 was expressed in Escherichia coli as Glutathione S-transferase fusion and purified by affinity chromatography. The phage library was then screened on this immobilized protein target. After three rounds of panning, phages were sequenced and shown to contain a consensus sequence NPNSAQG. Thereafter, either free p53 liberated from the fusion protein through thrombin treatment or Histidine-tagged p53 were recognized efficiently by the selected phage. To locate the p53-binding epitope of the selected hepta-peptide, three long peptides parts of the three known domains of the protein were synthesized and screened by the selected phage/peptide. Thus, the Carboxy-terminal p53 region was shown to be the target of the isolated phage as well as by its derived Fluorescein isothiocyanate-peptide. Molecular docking showed Lysine 386 as an important residue potentially engaged in this interaction. The selected hepta-peptide is a novel p53-interacting peptide, not described by other studies, and could be used as therapeutic tool in the future.
DOI: 10.1007/s10930-017-9730-1
PubMed: 28710679
Affiliations:
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Le document en format XML
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Tunisia.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratory of Eukaryotic Molecular Biotechnology, Center of Biotechnology of Sfax (CBS)/University of Sfax, Sidi Mansour, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author><author><name sortKey="Gargouri, Ali" sort="Gargouri, Ali" uniqKey="Gargouri A" first="Ali" last="Gargouri">Ali Gargouri</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Eukaryotic Molecular Biotechnology, Center of Biotechnology of Sfax (CBS)/University of Sfax, Sidi Mansour, Sfax, Tunisia. faouzi.gargouri@cbs.rnrt.tn.</nlm:affiliation><country xml:lang="fr">Tunisie</country><wicri:regionArea>Laboratory of Eukaryotic Molecular Biotechnology, Center of Biotechnology of Sfax (CBS)/University of Sfax, Sidi Mansour, Sfax</wicri:regionArea><wicri:noRegion>Sfax</wicri:noRegion></affiliation></author></analytic><series><title level="j">The protein journal</title><idno type="eISSN">1875-8355</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Apoptosis (MeSH)</term><term>Biotin (metabolism)</term><term>Escherichia coli (genetics)</term><term>Fluorescein-5-isothiocyanate (metabolism)</term><term>Glutathione Transferase (genetics)</term><term>Humans (MeSH)</term><term>Molecular Docking Simulation (MeSH)</term><term>Peptide Library (MeSH)</term><term>Peptides (chemistry)</term><term>Peptides (genetics)</term><term>Peptides (metabolism)</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Tumor Suppressor Protein p53 (chemistry)</term><term>Tumor Suppressor Protein p53 (genetics)</term><term>Tumor Suppressor Protein p53 (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Apoptose (MeSH)</term><term>Banque de peptides (MeSH)</term><term>Biotine (métabolisme)</term><term>Escherichia coli (génétique)</term><term>Fluorescéine-5-isothiocyanate (métabolisme)</term><term>Glutathione transferase (génétique)</term><term>Humains (MeSH)</term><term>Peptides (composition chimique)</term><term>Peptides (génétique)</term><term>Peptides (métabolisme)</term><term>Protéine p53 suppresseur de tumeur (composition chimique)</term><term>Protéine p53 suppresseur de tumeur (génétique)</term><term>Protéine p53 suppresseur de tumeur (métabolisme)</term><term>Protéines de fusion recombinantes (composition chimique)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Simulation de docking moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptides</term><term>Recombinant Fusion Proteins</term><term>Tumor Suppressor Protein p53</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutathione Transferase</term><term>Peptides</term><term>Recombinant Fusion Proteins</term><term>Tumor Suppressor Protein p53</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Biotin</term><term>Fluorescein-5-isothiocyanate</term><term>Peptides</term><term>Recombinant Fusion Proteins</term><term>Tumor Suppressor Protein p53</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peptides</term><term>Protéine p53 suppresseur de tumeur</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Glutathione transferase</term><term>Peptides</term><term>Protéine p53 suppresseur de tumeur</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Biotine</term><term>Fluorescéine-5-isothiocyanate</term><term>Peptides</term><term>Protéine p53 suppresseur de tumeur</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Apoptosis</term><term>Humans</term><term>Molecular Docking Simulation</term><term>Peptide Library</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Apoptose</term><term>Banque de peptides</term><term>Humains</term><term>Simulation de docking moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The transcription factor tumor protein p53 (P53) controls a variety of genes most involved in cell cycle and is at the origin of apoptosis when DNA is irreparably damaged. We planned to select novel tumor protein p53-interacting peptides through the screening of hepta-peptide phage-display libraries. For this aim, human tumor suppressor protein p53 was expressed in Escherichia coli as Glutathione S-transferase fusion and purified by affinity chromatography. The phage library was then screened on this immobilized protein target. After three rounds of panning, phages were sequenced and shown to contain a consensus sequence NPNSAQG. Thereafter, either free p53 liberated from the fusion protein through thrombin treatment or Histidine-tagged p53 were recognized efficiently by the selected phage. To locate the p53-binding epitope of the selected hepta-peptide, three long peptides parts of the three known domains of the protein were synthesized and screened by the selected phage/peptide. Thus, the Carboxy-terminal p53 region was shown to be the target of the isolated phage as well as by its derived Fluorescein isothiocyanate-peptide. Molecular docking showed Lysine 386 as an important residue potentially engaged in this interaction. The selected hepta-peptide is a novel p53-interacting peptide, not described by other studies, and could be used as therapeutic tool in the future.</div></front></TEI><affiliations><list><country><li>Tunisie</li></country></list><tree><country name="Tunisie"><noRegion><name sortKey="Ben Abid, Sihem" sort="Ben Abid, Sihem" uniqKey="Ben Abid S" first="Sihem" last="Ben Abid">Sihem Ben Abid</name></noRegion><name sortKey="Abdelmoula Souissi, Salma" sort="Abdelmoula Souissi, Salma" uniqKey="Abdelmoula Souissi S" first="Salma" last="Abdelmoula-Souissi">Salma Abdelmoula-Souissi</name><name sortKey="Gargouri, Ali" sort="Gargouri, Ali" uniqKey="Gargouri A" first="Ali" last="Gargouri">Ali Gargouri</name><name sortKey="Hassairi, Hajer" sort="Hassairi, Hajer" uniqKey="Hassairi H" first="Hajer" last="Hassairi">Hajer Hassairi</name><name sortKey="Mokdad Gargouri, Raja" sort="Mokdad Gargouri, Raja" uniqKey="Mokdad Gargouri R" first="Raja" last="Mokdad-Gargouri">Raja Mokdad-Gargouri</name><name sortKey="Sahnoun, Mouna" sort="Sahnoun, Mouna" uniqKey="Sahnoun M" first="Mouna" last="Sahnoun">Mouna Sahnoun</name><name sortKey="Yacoubi Hadj Amor, Ines" sort="Yacoubi Hadj Amor, Ines" uniqKey="Yacoubi Hadj Amor I" first="Ines" last="Yacoubi-Hadj Amor">Ines Yacoubi-Hadj Amor</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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