| Isolation of multiple cell-binding ligands from different phage displayed-peptide libraries. | |
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MedLine Citation:
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PMID: 16386888 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A technical challenge in the development of biosensor devices for cancer detection and diagnosis is the identification of ligands that recognize cancer cells with high affinity and specificity. Furthermore, it is unlikely that one cell-binding ligand will provide sufficient biological information, thus, multiple ligands for a given cancer type will be needed for confident clinical diagnosis. Biopanning of phage displayed peptide libraries is a route to isolation of specific cell-binding reagents. A potential approach towards isolation of multiple ligands for a single cell type is to pan against the same cell type using different peptide libraries. Here we report the synthesis of a new 20-mer peptide-phage library and its use to select a peptide that binds to the large cell lung carcinoma cell line, H1299. The isolated phage clone binds H1299 cells 80 times better than a control phage and can distinguish between H1299 and normal control cells. The phage clone also binds to the lung pleura epidermoid cell line, Calu-1 but not to all lung carcinoma cell lines. The peptide is functional outside the context of the phage and tetramerization of the peptide on a trilysine core improves the affinity of the peptide. The tetrameric peptide can be used to deliver a fluorescent quantum dot to H1299 cells. Unexpectedly, the peptide shares sequence similarity to a previously isolated H1299-binding peptide isolated from a different 20-mer peptide library. Data suggests that the two peptides target the same cellular receptor. Our results imply that cell-based biopanning can isolate cell-binding ligands that may be of utility for cancer diagnosis, and isolation of cell-targeting peptides from different peptide libraries can expand the repertoire of cell-binding reagents. |
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Authors:
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Tsukasa Oyama; Irene T Rombel; Kausar N Samli; Xin Zhou; Kathlynn C Brown |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2006-01-18 |
Journal Detail:
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Title: Biosensors & bioelectronics Volume: 21 ISSN: 0956-5663 ISO Abbreviation: Biosens Bioelectron Publication Date: 2006 Apr |
Date Detail:
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Created Date: 2006-03-27 Completed Date: 2009-06-03 Revised Date: 2009-07-14 |
Medline Journal Info:
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Nlm Unique ID: 9001289 Medline TA: Biosens Bioelectron Country: England |
Other Details:
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Languages: eng Pagination: 1867-75 Citation Subset: IM |
Affiliation:
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Division of Translational Research, Department of Internal Medicine, University of Texas Southwestern Medical Center, 5323 Harry Hines Building, Dallas, TX 75390-9185, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Binding Sites Cell Line, Tumor Humans Inovirus / chemistry*, metabolism* Ligands Molecular Sequence Data Peptide Library* Protein Binding |
| Grant Support | |
ID/Acronym/Agency:
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1 R01 CA 106646-01/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Ligands; 0/Peptide Library |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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