Brave new (strept)avidins in biotechnology

Trends in Biotechnology

Volumn 25, Issue 6, 2007, Pages 269-277

  Laitinen, Olli H ^a,d   Nordlund, Henri R ^b   Hytönen, Vesa P ^c   Kulomaa, Markku S ^b  

^a UNIVERSITY OF EASTERN FINLAND   (Finland)

^b UNIVERSITY OF TAMPERE   (Finland)

^c ETH ZURICH   (Switzerland)

^d Vactech Oy   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; BIOTECHNOLOGY; GENETIC ENGINEERING; PURIFICATION;

BIOSCIENCE; PROTEIN ENGINEERING;

PROTEINS;

AVIDIN; STREPTAVIDIN;

BIOMEDICINE; BIOTECHNOLOGY; CATALYST; CHIMERA; ENANTIOSELECTIVITY; GENETIC ENGINEERING; HUMAN; NANOTECHNOLOGY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN MODIFICATION; PROTEIN STABILITY; REVIEW;

BIOTECHNOLOGY; DRUG DESIGN; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN ENGINEERING; STREPTAVIDIN; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 34248570123     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2007.04.001     Document Type: Review

References (37)

1. Hanson C.V., et al. Catalytic antibodies and their applications. Curr. Opin. Biotechnol. 16 (2005) 631-636
2. Wilchek M., et al. Essentials of biorecognition: the (strept)avidin-biotin system as a model for protein-protein and protein-ligand interaction. Immunol. Lett. 103 (2006) 27-32
3. Laitinen O.H., et al. Genetically engineered avidins and streptavidins. Cell. Mol. Life Sci. 63 (2007) 2992-3017
4. Hytönen V.P., et al. Dual-affinity avidin molecules. Proteins 61 (2005) 597-607
5. Howarth M., et al. A monovalent streptavidin with a single femtomolar biotin-binding site. Nat. Methods 3 (2006) 267-273
6. Howarth M., et al. Targeting quantum dots to surface proteins in living cells with biotin ligase. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 7583-7588
7. Stayton P.S., et al. Smart polymer-streptavidin conjugates. Methods Mol. Biol. 283 (2004) 37-43
8. de Las Heras Alarcon C., et al. Stimuli responsive polymers for biomedical applications. Chem. Soc. Rev. 34 (2005) 276-285
9. Nordlund H.R., et al. Enhancing the thermal stability of avidin. Introduction of disulfide bridges between subunit interfaces. J. Biol. Chem. 278 (2003) 2479-2483
10. Laitinen O.H., et al. Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions. J. Biol. Chem. 276 (2001) 8219-8224
11. Laitinen O.H., et al. Rational design of an active avidin monomer. J. Biol. Chem. 278 (2003) 4010-4014
12. Wu S.C., and Wong S.L. Engineering soluble monomeric streptavidin with reversible biotin-binding capability. J. Biol. Chem. 280 (2005) 23225-23231
13. Nordlund H.R., et al. Production of Hev b5 as a fluorescent biotin-binding tripartite fusion protein in insect cells. Biochem. Biophys. Res. Commun. 336 (2005) 232-238
14. Carlson J.C., et al. Chemically controlled self-assembly of protein nanorings. J. Am. Chem. Soc. 128 (2006) 7630-7638
15. Nordlund H.R., et al. Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding. FEBS Lett. 555 (2003) 449-454
16. Niskanen E.A., et al. Chicken genome analysis reveals novel genes encoding biotin-binding proteins related to avidin family. BMC Genomics 6 (2005) 41
17. Hytönen V.P., et al. Chicken avidin-related protein 4/5 shows superior thermal stability when compared with avidin while retaining high affinity to biotin. J. Biol. Chem. 279 (2004) 9337-9343
18. Hytönen V.P., et al. Design and construction of highly stable, protease-resistant chimeric avidins. J. Biol. Chem. 280 (2005) 10228-10233
19. Prizant M., et al. Factors dictating the pseudocatalytic efficiency of avidins. J. Mol. Biol. 358 (2006) 754-763
20. Eisenberg-Domovich Y., et al. Structural elements responsible for conversion of streptavidin to a pseudoenzyme. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 5916-5921
21. Paganelli G., et al. Radioimmunotherapy of brain tumor. Neurol. Res. 28 (2006) 518-522
22. Thomas C.M., and Ward T.R. Artificial metalloenzymes: proteins as hosts for enantioselective catalysis. Chem. Soc. Rev. 34 (2005) 337-346
23. Klein G., et al. Tailoring the active site of chemzymes by using a chemogenetic-optimization procedure: towards substrate-specific artificial hydrogenases based on the biotin-avidin technology. Angew. Chem. Int. Ed. Engl. 44 (2005) 7764-7767
24. Letondor C., et al. Artificial transfer hydrogenases based on the biotin-(strept)avidin technology: fine tuning the selectivity by saturation mutagenesis of the host protein. J. Am. Chem. Soc. 128 (2006) 8320-8328
25. Schou C., and Heegaard N.H. Recent applications of affinity interactions in capillary electrophoresis. Electrophoresis 27 (2006) 44-59
26. Kitagawa F., et al. Chiral separation of acidic drug components by open tubular electrochromatography using avidin-immobilized capillaries. J. Chromatogr. A. 1130 (2006) 219-226
27. Gu J., et al. Nanometric protein arrays on protein-resistant monolayers on silicon surfaces. J. Am. Chem. Soc. 126 (2004) 8098-8099
28. Nordlund H.R., et al. Construction of a dual-chain pseudotetrameric chicken avidin by combining two circularly permuted avidins. J. Biol. Chem. 279 (2004) 36715-36719
29. Hytönen V.P., et al. Controlling quaternary structure assembly: subunit interface engineering and crystal structure of dual-chain avidin. J. Mol. Biol. 359 (2006) 1352-1363
30. Nordlund H.R., et al. Tetravalent single-chain avidin: from subunits to protein domains via circularly permuted avidins. Biochem. J. 392 (2005) 485-491
31. Aslan F.M., et al. Engineered single-chain dimeric streptavidins with an unexpected strong preference for biotin-4-fluorescein. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8507-8512
32. Park S., et al. A new set of molecular mechanics parameters for hydroxyproline and its use in molecular dynamics simulations of collagen-like peptides. J. Comput. Chem. 26 (2005) 1612-1616
33. Zocchi A., et al. Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris. Protein Expr. Purif. 32 (2003) 167-174
34. Christeller J.T., et al. 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. Insect Physiol. 51 (2005) 1117-1126
35. Wu S.C., and Wong S.L. Intracellular production of a soluble and functional monomeric streptavidin in Escherichia coli and its application for affinity purification of biotinylated proteins. Protein Expr. Purif. 46 (2006) 268-273
36. Hytönen V.P., et al. Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli. Biochem. J. 384 (2004) 385-390
37. Humphrey W., et al. VMD: visual molecular dynamics. J. Mol. Graph. 14 (1996) 33-38