Brave new (strept)avidins in biotechnology

被引:154
作者
Laitinen, Olli H.
Nordlund, Henri R.
Hytoenen, Vesa P.
Kulomaa, Markku S.
机构
[1] Univ Tampere, Inst Med Technol, FI-33014 Tampere, Finland
[2] Univ Kuopio, AI Virtanen Inst, FI-70211 Kuopio, Finland
[3] ETH, Dept Mat, CH-8093 Zurich, Switzerland
基金
芬兰科学院;
关键词
D O I
10.1016/j.tibtech.2007.04.001
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
Avidin and streptavidin are widely used in (strept) avidin-biotin technology, which is based on their tight biotin-binding capability. These techniques are exceptionally diverse, ranging from simple purification and labeling methods to sophisticated drug pre-targeting and nanostructure-building approaches. Improvements in protein engineering have provided new possibilities to develop tailored protein tools. The (strept)avidin scaffold has been engineered to extend the existing range of applications and to develop new ones. Modifications to (strept)avidins - such as simple amino acid substitutions to reduce biotin binding and alter physico-chemical characters - have recently developed into more sophisticated changes, including chimeric (strept)avidins, topology rearrangements and stitching of non-natural amino acids into the active sites. In this review, we highlight the current status in genetically engineered (strept)avidins and illustrate their versatility as advanced tools in the multiple fields of modern bioscience, medicine and nanotechnology.
引用
收藏
页码:269 / 277
页数:9
相关论文
共 37 条
[1]   Stimuli responsive polymers for biomedical applications [J].
Alarcón, CDH ;
Pennadam, S ;
Alexander, C .
CHEMICAL SOCIETY REVIEWS, 2005, 34 (03) :276-285
[2]   Engineered single-chain dimeric streptavidins with an unexpected strong preference for biotin-4-fluorescein [J].
Aslan, FM ;
Yu, Y ;
Mohr, SC ;
Cantor, CR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (24) :8507-8512
[3]   Chemically controlled self-assembly of protein nanorings [J].
Carlson, Jonathan C. T. ;
Jena, Sidhartha S. ;
Flenniken, Michelle ;
Chou, Tsui-fen ;
Siegel, Ronald A. ;
Wagner, Carston R. .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2006, 128 (23) :7630-7638
[4]   Distribution and residual activity of two insecticidal proteins, avidin and aprotinin, expressed in transgenic tobacco plants, in the bodies and frass of Spodoptera litura larvae following feeding [J].
Christeller, JT ;
Malone, LA ;
Todd, JH ;
Marshall, RM ;
Burgess, EPJ ;
Philip, BA .
JOURNAL OF INSECT PHYSIOLOGY, 2005, 51 (10) :1117-1126
[5]   Structural elements responsible for conversion of streptavidin to a pseudoenzyme [J].
Eisenberg-Domovich, Y ;
Pazy, Y ;
Nir, O ;
Raboy, B ;
Bayer, EA ;
Wilchek, M ;
Livnah, O .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (16) :5916-5921
[6]   Nanometric protein arrays on protein-resistant monolayers on silicon surfaces [J].
Gu, JH ;
Yam, CM ;
Li, S ;
Cai, CZ .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2004, 126 (26) :8098-8099
[7]   Catalytic antibodies and their applications [J].
Hanson, CV ;
Nishiyama, Y ;
Paul, S .
CURRENT OPINION IN BIOTECHNOLOGY, 2005, 16 (06) :631-636
[8]   A monovalent streptavidin with a single femtomolar biotin binding site [J].
Howarth, M ;
Chinnapen, DJF ;
Gerrow, K ;
Dorrestein, PC ;
Grandy, MR ;
Kelleher, NL ;
El-Husseini, A ;
Ting, AY .
NATURE METHODS, 2006, 3 (04) :267-273
[9]   Targeting quantum dots to surface proteins in living cells with biotin ligase [J].
Howarth, M ;
Takao, K ;
Hayashi, Y ;
Ting, AY .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2005, 102 (21) :7583-7588
[10]   VMD: Visual molecular dynamics [J].
Humphrey, W ;
Dalke, A ;
Schulten, K .
JOURNAL OF MOLECULAR GRAPHICS & MODELLING, 1996, 14 (01) :33-38