Isolation of leptin-binding peptides from a random peptide phage library
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چکیده
منابع مشابه
Puzzling Peptides from a Phage Display Library
The commercial availability of random peptide libraries displayed on the M13 phage is increasing their use forstudies on epitope identification, enzyme inhibitors, receptor ligands, etc. In this study two experimentswhere planned for selection of peptides. First with sheep antibodies, the positive selector was IgG, preparedon Protein G column from a pool of 11 sheeps immunized...
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The aim of this study was to screen for polypeptides binding specifically to LoVo human colorectal cancer cells using a phage-displayed peptide library as a targeting vector for colorectal cancer therapy. Human normal colorectal mucous epithelial cells were applied as absorber cells for subtraction biopanning with a c7c phage display peptide library. Positive phage clones were identified by enz...
متن کاملIdentification of high-affinity VEGFR3-binding peptides through a phage-displayed random peptide library
OBJECTIVE Vascular endothelial growth factor (VEGF) interaction with its receptor, VEGFR-3/Flt-4, regulates lymphangiogenesis. VEGFR-3/Flt-4 expression in cancer cells has been correlated with clinical stage, lymph node metastasis, and lymphatic invasion. The objective of this study is to identify a VEGFR-3/Flt-4-interacting peptide that could be used to inhibit VEGFR-3 for ovarian cancer thera...
متن کاملIsolation of peptides that inhibit binding of basic fibroblast growth factor to its receptor from a random phage-epitope library.
Basic fibroblast growth factor (bFGF) is known to bind to its cell-surface receptors with high affinity and in a heparin-dependent manner. In an attempt to predict the receptor recognition site on bFGF we screened phage-epitope libraries with monoclonal antibodies DG2 and DE6, which inhibit bFGF binding to its receptor. On the affinity-isolated phages, we identified several peptide sequences as...
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ژورنال
عنوان ژورنال: The Journal of Peptide Research
سال: 2000
ISSN: 1397-002X
DOI: 10.1034/j.1399-3011.2000.00679.x