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Literature DB >> 12413859

A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library.

Changshou Gao¹, Shenlan Mao, Henrik J Ditzel, Lauge Farnaes, Peter Wirsching, Richard A Lerner, Kim D Janda.

Abstract

A novel random peptide library was constructed using a phage-display format on the coat proteins pVII and pIX of filamentous bacteriophage. Panning against B-lymphocyte WI-L2 cells yielded one unique peptide-phage, denoted CHL8, that specifically bound to and penetrated the cells. Studies of each peptide derived from CHL8, denoted pep7 and pep9, established that only pep7 mediated the observed activity and only as a homodimer. Peptide libraries displayed on pVII-pIX should serve as a novel source of bioactive ligands for a variety of applications.

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Year: 2002 PMID： 12413859 DOI： 10.1016/s0968-0896(02)00340-1

Source DB: PubMed Journal: Bioorg Med Chem ISSN： 0968-0896 Impact factor: 3.641

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Cited

13 in total

10. Cellular internalization mechanism and intracellular trafficking of filamentous M13 phages displaying a cell-penetrating transbody and TAT peptide.

Authors: Aeyung Kim; Tae-Hwan Shin; Seung-Min Shin; Chuong D Pham; Dong-Ki Choi; Myung-Hee Kwon; Yong-Sung Kim
Journal: PLoS One Date: 2012-12-14 Impact factor: 3.240

A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library.

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10. Cellular internalization mechanism and intracellular trafficking of filamentous M13 phages displaying a cell-penetrating transbody and TAT peptide.