In vitro selection of nucleic acids and proteins:: what are we learning?

被引:34
作者
Roberts, RW [1 ]
Ja, WW [1 ]
机构
[1] CALTECH, Div Chem & Chem Engn, Pasadena, CA 91125 USA
关键词
D O I
10.1016/S0959-440X(99)80074-8
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
For almost a decade, in vitro selection experiments have been used to isolate novel nucleic acids, peptides and proteins according to their function. Selection experiments have altered our perception of molecular mimicry and catalysis, and they appear to be more facile than rational design at generating biopolymers with desired properties. New methods that have been developed improve the power of functional strategies in ways that nature has already discovered - by expanding library size and facilitating the recombination of positive mutations. Recent structural information on a number of selected and evolved molecules highlights future challenges far design via rational approaches.
引用
收藏
页码:521 / 529
页数:9
相关论文
共 112 条
[1]   Probing the importance of second sphere residues in an esterolytic antibody by phage display [J].
Arkin, MR ;
Wells, JA .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 284 (04) :1083-1094
[2]   Phage display of a catalytic antibody to optimize affinity for transition-state analog binding [J].
Baca, M ;
Scanlan, TS ;
Stephenson, RC ;
Wells, JA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (19) :10063-10068
[3]   Selection of heregulin variants having higher affinity for the ErbB3 receptor by monovalent phage display [J].
Ballinger, MD ;
Jones, JT ;
Lofgren, JA ;
Fairbrother, WJ ;
Akita, RW ;
Sliwkowski, MX ;
Wells, JA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (19) :11675-11684
[4]   Immune versus natural selection: Antibody aldolases with enzymic rates but broader scope [J].
Barbas, CF ;
Heine, A ;
Zhong, GF ;
Hoffmann, T ;
Gramatikova, S ;
Bjornestedt, R ;
List, B ;
Anderson, J ;
Stura, EA ;
Wilson, IA ;
Lerner, RA .
SCIENCE, 1997, 278 (5346) :2085-2092
[5]   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
[6]  
Breaker R R, 1994, Chem Biol, V1, P223, DOI 10.1016/1074-5521(94)90014-0
[7]   In vitro selection of catalytic polynucleotides [J].
Breaker, RR .
CHEMICAL REVIEWS, 1997, 97 (02) :371-390
[8]   Selection of phage displayed peptides from a random 10-mer library recognising a peptide target [J].
Bremnes, T ;
Lauvrak, V ;
Lindqvist, B ;
Bakke, O .
IMMUNOTECHNOLOGY, 1998, 4 (01) :21-28
[9]   In vitro selection of self-cleaving DNAs [J].
Carmi, N ;
Shultz, LA ;
Breaker, RR .
CHEMISTRY & BIOLOGY, 1996, 3 (12) :1039-1046
[10]   A HOT-SPOT OF BINDING-ENERGY IN A HORMONE-RECEPTOR INTERFACE [J].
CLACKSON, T ;
WELLS, JA .
SCIENCE, 1995, 267 (5196) :383-386