Optimizing the affinity and specificity of proteins with molecular display

被引：87

作者：

Levin, AM ^{[1
]}

Weiss, GA ^{[1
]}

机构：

[1] Univ Calif Irvine, Dept Chem, Irvine, CA 92697 USA

来源：

MOLECULAR BIOSYSTEMS | 2006年 / 2卷 / 01期

关键词：

D O I：

10.1039/b511782h

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Affinity maturation of receptor-ligand interactions represents an important area of academic and pharmaceutical research. Improving affinity and specificity of proteins can tailor potency for both in vivo and in vitro, applications. A number of different display platforms including phage display, bacterial and yeast display, ribosome display, and mRNA display can optimize protein affinity and specificity. Here, we will review the advantages and disadvantages of these molecular display methods with a focus on their suitability for protein affinity maturation.

引用

收藏

页码：49 / 57

页数：9

相关论文

共 112 条

[41] Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display [J].

Hanes, J ;

Schaffitzel, C ;

Knappik, A ;

Plückthun, A .

NATURE BIOTECHNOLOGY, 2000, 18 (12) :1287-1292

[42] SELECTION OF PHAGE ANTIBODIES BY BINDING-AFFINITY - MIMICKING AFFINITY MATURATION [J].

HAWKINS, RE ;

RUSSELL, SJ ;

WINTER, G .

JOURNAL OF MOLECULAR BIOLOGY, 1992, 226 (03) :889-896

[43] In vitro antibody evolution targeting germline hot spots to increase activity of an anti-CD22 immunotoxin [J].

Ho, M ;

Kreitman, RJ ;

Onda, M ;

Pastan, I .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (01) :607-617

[44] In vitro evolution of a T cell receptor with high affinity for peptide/MHC [J].

Holler, PD ;

Holman, PO ;

Shusta, EV ;

O'Herrin, S ;

Wittrup, KD ;

Kranz, DM .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (10) :5387-5392

[45] TCRs with high affinity for foreign pMHC show self-reactivity [J].

Holler, PD ;

Chlewicki, LK ;

Kranz, DM .

NATURE IMMUNOLOGY, 2003, 4 (01) :55-62

[46] MULTISUBUNIT PROTEINS ON THE SURFACE OF FILAMENTOUS PHAGE - METHODOLOGIES FOR DISPLAYING ANTIBODY (FAB) HEAVY AND LIGHT-CHAINS [J].

HOOGENBOOM, HR ;

GRIFFITHS, AD ;

JOHNSON, KS ;

CHISWELL, DJ ;

HUDSON, P ;

WINTER, G .

NUCLEIC ACIDS RESEARCH, 1991, 19 (15) :4133-4137

[47] Changes in the specificity of antibodies against steroid antigens by introduction of mutations into complementarity-determining regions of the VH domain [J].

Iba, Y ;

Hayashi, N ;

Sawada, J ;

Titani, K ;

Kurosawa, Y .

PROTEIN ENGINEERING, 1998, 11 (05) :361-370

[48] A rapid, generally applicable method to engineer zinc fingers illustrated by targeting the HIV-1 promoter [J].

Isalan, M ;

Klug, A ;

Choo, Y .

NATURE BIOTECHNOLOGY, 2001, 19 (07) :656-660

[49] Tailoring in vitro evolution for protein affinity or stability [J].

Jermutus, L ;

Honegger, A ;

Schwesinger, F ;

Hanes, J ;

Plückthun, A .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (01) :75-80

[50] Directed evolution, phage display and combination of evolved mutants:: A strategy to recover the neutralization properties of the scFv version of BCF2 a neutralizing monoclonal antibody specific to scorpion toxin Cn2 [J].

Juárez-González, VR ;

Riaño-Umbarila, L ;

Quintero-Hernández, V ;

Olamendi-Portugal, T ;

Ortiz-León, M ;

Ortíz, E ;

Possan, LD ;

Becerril, B .

JOURNAL OF MOLECULAR BIOLOGY, 2005, 346 (05) :1287-1297

← 1 2 3 4 5 6 7 8 9 10 →