Artificial, non-antibody binding proteins for pharmaceutical and industrial applications

被引:92
作者
Hey, T
Fiedler, E
Rudolph, R
Fiedler, M
机构
[1] Univ Halle Wittenberg, Inst Biotechnol, D-06120 Halle An Der Saale, Germany
[2] Scil Prot GmbH, D-06120 Halle An Der Saale, Germany
关键词
D O I
10.1016/j.tibtech.2005.07.007
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Using combinatorial chemistry to generate novel binding molecules based on protein frameworks ('scaffolds') is a concept that has been strongly promoted during the past five years in both academia and industry. Non-antibody recognition proteins derive from different structural families and mimic the binding principle of immunoglobulins to varying degrees. In addition to the specific binding of a pre-defined target, these proteins provide favourable characteristics such as robustness, ease of modification and cost-efficient production. The broad spectrum of potential applications, including research tools, separomics, diagnostics and therapy, has led to the commercial exploitation of this technology by various small- and medium-sized companies. It is predicted that scaffold-based affinity reagents will broaden and complement applications that are presently covered by natural or recombinant antibodies. Here, we provide an overview on current approaches in the biotech industry, considering both scientific and commercial aspects.
引用
收藏
页码:514 / 522
页数:9
相关论文
共 78 条
[1]   Transferrin Trojan horses as a rational approach for the biological delivery of therapeutic peptide domains [J].
Ali, SA ;
Joao, HC ;
Hammerschmid, F ;
Eder, J ;
Steinkasserer, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (34) :24066-24073
[2]   Inclusion of a non-immunoglobulin binding protein in two-site ELISA for quantification of human serum proteins without interference by heterophilic serum antibodies [J].
Andersson, M ;
Rönnmark, J ;
Areström, I ;
Nygren, PÅ ;
Ahlborg, N .
JOURNAL OF IMMUNOLOGICAL METHODS, 2003, 283 (1-2) :225-234
[3]   Identification of epitope-like consensus motifs using mRNA display [J].
Baggio, R ;
Burgstaller, P ;
Hale, SP ;
Putney, AR ;
Lane, M ;
Lipovsek, D ;
Wright, MC ;
Roberts, RW ;
Liu, RH ;
Szostak, JW ;
Wagner, RW .
JOURNAL OF MOLECULAR RECOGNITION, 2002, 15 (03) :126-134
[4]   Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold [J].
Beste, G ;
Schmidt, FS ;
Stibora, T ;
Skerra, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (05) :1898-1903
[5]   High-affinity binders selected from designed ankyrin repeat protein libraries [J].
Binz, HK ;
Amstutz, P ;
Kohl, A ;
Stumpp, MT ;
Briand, C ;
Forrer, P ;
Grütter, MG ;
Plückthun, A .
NATURE BIOTECHNOLOGY, 2004, 22 (05) :575-582
[6]   Designing repeat proteins:: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins [J].
Binz, HK ;
Stumpp, MT ;
Forrer, P ;
Amstutz, P ;
Plückthun, A .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 332 (02) :489-503
[7]   Antibodies from phage antibody libraries [J].
Bradbury, ARM ;
Marks, JD .
JOURNAL OF IMMUNOLOGICAL METHODS, 2004, 290 (1-2) :29-49
[8]   RENATURATION, PURIFICATION AND CHARACTERIZATION OF RECOMBINANT FAB-FRAGMENTS PRODUCED IN ESCHERICHIA-COLI [J].
BUCHNER, J ;
RUDOLPH, R .
BIO-TECHNOLOGY, 1991, 9 (02) :157-162
[9]   Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates [J].
Caliceti, P ;
Veronese, FM .
ADVANCED DRUG DELIVERY REVIEWS, 2003, 55 (10) :1261-1277
[10]   Selection and analysis of an optimized anti-VEGF antibody: Crystal structure of an affinity-matured Fab in complex with antigen [J].
Chen, Y ;
Wiesmann, C ;
Fuh, G ;
Li, B ;
Christinger, HW ;
McKay, P ;
de Vos, AM ;
Lowman, HB .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 293 (04) :865-881