BACTERIOPHAGE-M-13 DISPLAYING DISULFIDE-CONSTRAINED MICROPROTEINS

被引：145

作者：

MCLAFFERTY, MA ^{[1
]}

KENT, RB ^{[1
]}

LADNER, RC ^{[1
]}

MARKLAND, W ^{[1
]}

机构：

[1] PROT ENGN CORP,765 CONCORD AVE,CAMBRIDGE,MA 02138

来源：

GENE | 1993年 / 128卷 / 01期

关键词：

SINGLE-STRANDED BACTERIOPHAGE; LIBRARY SCREENING; STREPTAVIDIN; ANTI-BETA-ENDORPHIN MONOCLONAL ANTIBODY; RECOMBINANT DNA;

D O I：

10.1016/0378-1119(93)90149-W

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

A display-phage library (TN2), displaying an 18-residue peptide fused to coat protein III, represents a collection of up to 8.55 X 10(6) peptides encoded by only 1.68 x 10(7) DNA sequences. Each displayed peptide has two fixed cysteine residues (allowing disulfide formation) and six variegated residues, four between the cysteines and one either side of the cysteines. Screening this library against streptavidin (Sv) and the anti-beta-endorphin monoclonal antibody, 3-E7, yielded phage displaying disulfide-constrained microproteins with sequences similar to those published for the linear-peptide display phage. Analysis of selected clones indicated that a disulfide bond is required for high-affinity binding to each of the target proteins. The microproteins selected for binding to Sv and 3-E7 show more stringent sequence specificity than do linear peptides selected for binding to the same targets.

引用

页码：29 / 36

页数：8

共 17 条

[1] HORMONE PHAGE - AN ENRICHMENT METHOD FOR VARIANT PROTEINS WITH ALTERED BINDING-PROPERTIES [J].