Display random peptide

Yao, Z.-J., Kao, M. C. C., and Chung, M. C. M. (1995). Epitope identification by polyclonal antibody from phage-displayed random peptide library. J. Protein Chem. 14, 161-166. 

We have previously developed an in vivo selection method in which peptides that home to specific vascular beds are selected after intravenous administration of a phage display random peptide library [5]. This strategy revealed a vascular address system that allows tissue-specific targeting of normal blood vessels [6-8] and angiogenesis-related targeting of tumor blood vessels [3, 6, 9-12]. While the biologi-... 

Another form of displayed peptide library is the FliTrx Random Peptide Display Library (Invitrogen, Paisley, UK), which uses the bacterial flagellum to display random peptide libraries on the E. coli cell surface (14). This library was constructed in the pFliTrx vector, which positions the random peptides in a flagellin (Fli) thioredoxin (Trx) fusion protein. Biopanning with bacteria works surprisingly well in our experience (15) and screening on nitrocellulose is similar to the Smith method. 

Sparks AB, Quilliam LA, Thorn JM, Der CJ, Kay BK, Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries, J. Biol. Chem., 269(39) 23853-23856, 1994. 

A phage-displayed random peptide library expressing pen-tadecamer amino acid residues at the N terminus of pill phage coat protein of Ml 3 phage was kindly provided by Dr. Hideyuki Saya at Keio University. 

This is sufficient time to allow for binding of the phage displaying random peptides to the normal vasculature and other nontumor antigens, but not enough time for the phage to extravasate into the tissues (10). 

This perfusion reduces phage from the vasculature space, thus facilitating the selection of phage displaying random peptides, which directly bind to the tissue/tumor of interest. 

J.M. Davies, et al., (1999). Multiple alignment and sorting of peptides derived from phage-displayed random peptide libraries with polyclonal sera allows discrimination of relevant phagotopes. Mol. Immunol. 36, 659-667. 

Sparks, A. B., Rider, J. E., and Kay, B. K. (1998). Mapping the specificity of SHS domains with phage-displayed random-peptide libraries. Methods Mol. Biol. 84, 87-103. 

A. Sahu, B. K. Kay, and J. D. Lambris, Inhibition of human complement by a c3-binding peptide isolated from a phage-displayed random peptide hbrary. J. Immunol. 157, 884-891 (1996). 

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