@article{oai:kindai.repo.nii.ac.jp:00011493,
 author = {森田,  資隆},
 issue = {11},
 journal = {かやのもり：近畿大学産業理工学部研究報告, Reports of School of Humanity-Oriented Science and Engineering, Kinki University},
 month = {Nov},
 note = {[Abstract] Phage display peptide library is based on a combinatorial library of random peptide fused to a minor coat protein of the filamentous M13 phage. Phage display creates a physical linkage between a displayed selectable function and the DNA encoding that function. This allows rapid identification of peptide ligands for a variety of target molecules by an in vitro selection process. Phage display is an effective technique for isolation of the peptides and proteins, that can bind to a specific mole cule. In the selection of a phage, not only purified prote insimmobilized on an article surface or intact cells, but also chemical molecules or a surface have been used as the target. This approach makes it possible to use chemicals in physiological condition as the target, so that phage display is suitable for the development of peptides that bind to a molecular antigen. The peptide isolated from a phage display library could conjugate with a particular dye, which makes it applicable to identification and isolation of specific chemicals.      To the best of our knowledge, this report is the first attempt to develop a peptide, that can recognize fullerene(C60). Features of peptide isolation from a phage display library are discussed in the following sessions. Furthermore, the peptide that sense the one of the dioxin, 2,3,7-trichlorodibenzo-p-dioxin (2,3,7-TCDD), or the peptide from phage display peptide library, one of combinatorial technology, could bind to the undifferentiated P19 cells were isolated and characterized., application/pdf},
 pages = {1--7},
 title = {<総説>バイオセンシング素子としてのコンビナトリアルペプチドの応用},
 year = {2009},
 yomi = {モリタ, ヤスタカ}
}