Screening for transient biological interactions as applied to albumin ligands: A new concept for drug discovery

Analytical Biochemistry

Volumn 359, Issue 1, 2006, Pages 120-123

  Ohlson, Sten ^a   Shoravi, Siamak ^a   Fex, Tomas ^b   Isaksson, Roland ^a  

^a LINNAEUS UNIVERSITY   (Sweden)

^b ASTRAZENECA R AND D   (Sweden)

Author keywords

Drug discovery; High throughput screening; Transient interactions; Weak affinity; Weak affinity chromatography

Indexed keywords

AFFINITY CHROMATOGRAPHY; BINDERS; DISSOCIATION;

AFFINITY SELECTION; BIOLOGICAL INTERACTIONS; BIOLOGICAL SCIENCE; DISSOCIATION CONSTANT; DRUG DISCOVERY; HIGH THROUGHPUT SCREENING; TRANSIENT INTERACTIONS; WEAK AFFINITY;

DRUG INTERACTIONS;

BOVINE SERUM ALBUMIN; BUPIVACAINE; PROPRANOLOL; SODIUM AZIDE;

ARTICLE; BINDING AFFINITY; BINDING KINETICS; CHROMATOGRAPHY; DISSOCIATION CONSTANT; DRUG RESEARCH; HIGH THROUGHPUT SCREENING; MOLECULAR INTERACTION; PRIORITY JOURNAL;

EID: 33750606868     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2006.09.007     Document Type: Article

References (30)

1. In: Gabius H.-J., and Gabius S. (Eds). Glycosciences: Status and Perspectives (1997), Chapman & Hall, Weinheim 44-88
2. Zopf D., and Ohlson S. Weak-affinity chromatography. Nature 346 (1990) 87-88
3. Strandh M., Andersson H., and Ohlson S. In: Bailon P., Ehrlich G.K., Fung W.J., and Berthold W. (Eds). Methods in Molecular Biology (2000), Humana Press, Inc, Totowa, NJ 7-24
4. Nilsson M., et al. Determination of protein-ligand affinity constants from direct migration time in capillary electrophoresis. Electrophoresis 25 (2004) 1829-1836
5. MacKenzie C.R., et al. Analysis by surface plasmon resonance of the influence of valence on the ligand binding affinity and kinetics of an anti-carbohydrate antibody. J. Biol. Chem. 271 (1996) 1527-1533
6. Engström H.A., Andersson P.O., and Ohlson S. Analysis of the specificity and thermodynamics of the interaction between low affinity antibodies and carbohydrate antigens using fluorescence spectroscopy. J. Immunol. Methods 297 (2005) 203-211
7. Pellechia M., Sem D.S., and Wuthrich K. NMR in drug discovery. Nat. Rev. Drug Discov. 1 (2002) 211-219
8. Plotnikov V., et al. An autosampling differential scanning calorimeter instrument for studying molecular interactions. Assay Drug Dev. Technol. 1 (2002) 83-90
9. Causey L.D., and Dwyer D.S. Detection of low affinity interactions between peptides and heat shock proteins by chemiluminescence of enhanced avidity reactions (CLEAR). Nat. Biotechnol. 14 (1996) 348-351
10. Mammen M., Choi S.-K., and Whitesides G.M. Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors. Angew. Chem. Int. Ed. 37 (1998) 2754-2794
11. Dustin M.L., et al. Low affinity interaction of human or rat T cell adhesion molecule CD2 with its ligand aligns adhering membranes to achieve high physiological affinity. J. Biol. Chem. 272 (1997) 30889-30898
12. Karjalainen K. High-sensitivity, low affinity-paradox of T-cell receptor recognition. Curr. Opin. Immunol. 6 (1994) 9-12
13. Beeson C., et al. Early biochemical signals arise from low affinity TCR-ligand reactions as the cell-cell interface. J. Exp. Med. 184 (1996) 777-782
14. Garcia C.D., DeGail J.H., Wilson W.W., and Henry C.S. Measuring protein interactions by microchip self-interaction chromatography. Biotechnol. Prog. 19 (2003) 1006-1010
15. Zopf D., and Roth S. Oligosaccharide anti-infective agents. Lancet 347 (1996) 1017-1021
16. Elgavish S., and Shaanan B. Lectin-carbohydrate interactions: different folds, common recognition principles. Trends Biochem. Sci. 22 (1997) 462-467
17. Fuente J.M.d.l., and Penadés S. Understanding carbohydrate-carbohydrate interactions by means of glyconanotechnology. Glycoconj. J. 21 (2004) 149-163
18. Ohlson S., Jungar C., Strandh M., and Mandenius C.-F. Continuous weak-affinity immunosensing. Trends Biotechnol. 18 (2000) 49-52
19. Regenmortel M.H.V.V. From absolute to exquisite specificity. Reflections on the fuzzy nature of species, specificity and antigenic sites. J. Immunol. Methods 216 (1998) 37-48
20. Leickt L., Grubb A., and Ohlson S. Development of monoclonal antibodies against creatine kinase CKMB2. Scand J. Clin. Lab. Invest. 62 (2002) 423-430
21. Frantz S. Drug discovery: playing dirty. Nature 437 (2005) 942-943
22. Erlanson D.A., McDowell R.S., and O'Brien T. Fragment-based drug discovery. J. Med. Chem. 47 (2004) 3463-3482
23. Erickson J.A., Jalaie M., Robertson D.H., Lewis R.A., and Vieth M. Lessons in molecular recognition: the effects of ligand and protein flexibility on docking accuracy. J. Med. Chem. 47 (2004) 45-55
24. Sundberg S.A. High-throughput and ultra-high-throughput screening: solution- and cell-based approaches. Curr. Opin. Biotechnol. 11 (2000) 47-53
25. Williams G.P. Advances in high throughput screening. Drug Disco. Today 9 (2004) 515-516
26. Chan N.W.C., Lewis D.F., Rosner P.J., Kelly M.A., and Schriemer D.C. Frontal affinity chromatography-mass spectrometry assay technology for multiple stages of drug discovery: applications of a chromatographic biosensor. Anal. Chem. 319 (2003) 1-12
27. Ohlson S., Lundblad A., and Zopf D. Novel Approach to affinity chromatography using "weak" monoclonal antibodies. Anal. Biochem. 169 (1988) 204-208
28. Erlandsson P., Hansson L., and Isaksson R. Direct analytical and preparative resolution of enantiomers using albumin adsorbed to silica as a stationary phase. J. Chromatogr. 370 (1986) 475-483
29. Haginaka J. Protein-based chiral stationary phases for high-performance liquid chromatography enantioseparations. J. Chromatog. A. 906 (2001) 253-273
30. Lipton S.A., and Chen H.S. Paradigm shift in neuroprotective drug development: clinically tolerated NMDA receptor inhibition by memantine. Cell Death Different. 11 (2004) 18-20