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T7 lytic phage‐displayed peptide libraries exhibit less sequence bias than M13 filamentous phage‐displayed peptide libraries
Author(s) -
Krumpe Lauren R. H.,
Atkinson Andrew J.,
Smythers Gary W.,
Kandel Andrea,
Schumacher Kathryn M.,
McMahon James B.,
Makowski Lee,
Mori Toshiyuki
Publication year - 2006
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200500606
Subject(s) - peptide , phage display , lytic cycle , peptide library , streptavidin , biology , peptide sequence , computational biology , biochemistry , chemistry , genetics , biotin , gene , virus
We investigated whether the T7 system of phage display could produce peptide libraries of greater diversity than the M13 system of phage display due to the differing processes of lytic and filamentous phage morphogenesis. Using a bioinformatics‐assisted computational approach, collections of random peptide sequences obtained from a T7 12‐mer library (X 12 ) and a T7 7‐mer disulfide‐constrained library (CX 7 C) were analyzed and compared with peptide populations obtained from New England BioLabs' M13 Ph.D.‐12™ and Ph.D.‐C7C™ libraries. Based on this analysis, peptide libraries constructed with the T7 system have fewer amino acid biases, increased peptide diversity, and more normal distributions of peptide net charge and hydropathy than the M13 libraries. The greater diversity of T7‐displayed libraries provides a potential resource of novel binding peptides for new as well as previously studied molecular targets. To demonstrate their utility, several of the T7‐displayed peptide libraries were screened for streptavidin‐ and neutravidin‐binding phage. Novel binding motifs were identified for each protein.