Characterization of prostate‐specific antigen binding peptides selected by phage display technology
Identifieur interne : 002E49 ( Main/Exploration ); précédent : 002E48; suivant : 002E50Characterization of prostate‐specific antigen binding peptides selected by phage display technology
Auteurs : Catherine Ferrieu-Weisbuch [France] ; Sandrine Michel [France] ; Emilie Collomb-Clerc [France] ; Catherine Pothion [France] ; Gilbert Deléage [France] ; Colette Jolivet-Reynaud [France]Source :
- Journal of Molecular Recognition [ 0952-3499 ] ; 2006-01.
Abstract
Prostate‐specific antigen (PSA) is an important marker for the diagnosis and management of prostate cancer. Free PSA has been shown to be more extensively cleaved in sera from benign prostatic hyperplasia patients than in sera from prostate cancer patients. Moreover, the presence of enzymatically activatable PSA was characterized previously in sera from patients with prostate cancer by the use of the specific anti‐free PSA monoclonal antibody (mAb) 5D3D11. As an attempt to obtain ligands for the specific recognition of different PSA forms including active PSA, phage‐displayed linear and cyclic peptide libraries were screened with PSA coated directly into microplate wells or presented by two different anti‐total PSA mAbs. Four different phage clones were selected for their ability to recognize PSA and the inserted peptides were produced as synthetic peptides. These peptides were found to capture and to detect specifically free PSA, even in complex biological media such as sera or tumour cell culture supernatants. Alanine scanning of peptide sequences showed the involvement of aromatic and hydrophobic residues in the interaction of the peptides with PSA whereas Spotscan analysis of overlapping peptides covering the PSA sequence identified a peptide binding to the kallikrein loop at residues 82–87, suggesting that the peptides could recognize a non‐clipped form of PSA. Moreover, the PSA‐specific peptides enhance the enzymatic activity of PSA immobilized into microplate wells whereas the capture of PSA by the peptides inhibited totally its enzymatic activity while the peptide binding to PSA had no effect in solution. These PSA‐specific peptides could be potential tools for the recognition of PSA forms more specifically associated to prostate cancer. Copyright © 2005 John Wiley & Sons, Ltd.
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DOI: 10.1002/jmr.762
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Free PSA has been shown to be more extensively cleaved in sera from benign prostatic hyperplasia patients than in sera from prostate cancer patients. Moreover, the presence of enzymatically activatable PSA was characterized previously in sera from patients with prostate cancer by the use of the specific anti‐free PSA monoclonal antibody (mAb) 5D3D11. As an attempt to obtain ligands for the specific recognition of different PSA forms including active PSA, phage‐displayed linear and cyclic peptide libraries were screened with PSA coated directly into microplate wells or presented by two different anti‐total PSA mAbs. Four different phage clones were selected for their ability to recognize PSA and the inserted peptides were produced as synthetic peptides. These peptides were found to capture and to detect specifically free PSA, even in complex biological media such as sera or tumour cell culture supernatants. Alanine scanning of peptide sequences showed the involvement of aromatic and hydrophobic residues in the interaction of the peptides with PSA whereas Spotscan analysis of overlapping peptides covering the PSA sequence identified a peptide binding to the kallikrein loop at residues 82–87, suggesting that the peptides could recognize a non‐clipped form of PSA. Moreover, the PSA‐specific peptides enhance the enzymatic activity of PSA immobilized into microplate wells whereas the capture of PSA by the peptides inhibited totally its enzymatic activity while the peptide binding to PSA had no effect in solution. These PSA‐specific peptides could be potential tools for the recognition of PSA forms more specifically associated to prostate cancer. Copyright © 2005 John Wiley & Sons, Ltd.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Lyon</li><li>MARCY L'ETOILE</li></settlement></list><tree><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Ferrieu Eisbuch, Catherine" sort="Ferrieu Eisbuch, Catherine" uniqKey="Ferrieu Eisbuch C" first="Catherine" last="Ferrieu-Weisbuch">Catherine Ferrieu-Weisbuch</name></region><name sortKey="Collomb Lerc, Emilie" sort="Collomb Lerc, Emilie" uniqKey="Collomb Lerc E" first="Emilie" last="Collomb-Clerc">Emilie Collomb-Clerc</name><name sortKey="Deleage, Gilbert" sort="Deleage, Gilbert" uniqKey="Deleage G" first="Gilbert" last="Deléage">Gilbert Deléage</name><name sortKey="Jolivet Eynaud, Colette" sort="Jolivet Eynaud, Colette" uniqKey="Jolivet Eynaud C" first="Colette" last="Jolivet-Reynaud">Colette Jolivet-Reynaud</name><name sortKey="Jolivet Eynaud, Colette" sort="Jolivet Eynaud, Colette" uniqKey="Jolivet Eynaud C" first="Colette" last="Jolivet-Reynaud">Colette Jolivet-Reynaud</name><name sortKey="Jolivet Eynaud, Colette" sort="Jolivet Eynaud, Colette" uniqKey="Jolivet Eynaud C" first="Colette" last="Jolivet-Reynaud">Colette Jolivet-Reynaud</name><name sortKey="Michel, Sandrine" sort="Michel, Sandrine" uniqKey="Michel S" first="Sandrine" last="Michel">Sandrine Michel</name><name sortKey="Pothion, Catherine" sort="Pothion, Catherine" uniqKey="Pothion C" first="Catherine" last="Pothion">Catherine Pothion</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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