A cell-penetrating peptide from a novel pVII-pIX phage-displayed random peptide library.
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.
Gao
Changshou
C
Department of Chemistry, The Scripps Research Institute and the Skaggs Institute for Chemical Biology, La Jolla, CA 92037, USA.
Mao
Shenlan
S
Ditzel
Henrik J
HJ
Farnaes
Lauge
L
Wirsching
Peter
P
Lerner
Richard A
RA
Janda
Kim D
KD
D001402:B-Lymphocytes; D001435:Bacteriophages / Q000737:chemistry; D036022:Capsid Proteins / Q000737:chemistry* / Q000493:pharmacokinetics; D002460:Cell Line; D002462:Cell Membrane / Q000737:chemistry; D004705:Endocytosis; D006801:Humans; D019151:Peptide Library; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry / Q000493:pharmacokinetics*
D036022:Capsid Proteins; D019151:Peptide Library; D010455:Peptides; C119217:coat protein pVIII, Enterobacteria phage fd