Thermodynamically Stable Aggregation-Resistant Antibody Domains through Directed Evolution

Journal of Molecular Biology

Volumn 376, Issue 4, 2008, Pages 926-931

  Famm, Kristoffer ^a   Hansen, Lars ^a   Christ, Daniel ^b   Winter, Greg ^a  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

^b GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

aggregation; antibody domains; dAbs; directed evolution; phage display

Indexed keywords

ANTIBODY;

ARTICLE; DENATURATION; DIRECTED MOLECULAR EVOLUTION; PH; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY; THERMODYNAMICS;

PLEURONECTIDAE;

EID: 39049173446     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.10.075     Document Type: Article

References (23)

1. Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
2. Hecht M.H., Richardson J.S., Richardson D.C., and Ogden R.C. De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence. Science 249 (1990) 884-891
3. Wang W., and Hecht M.H. Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins. Proc. Natl Acad. Sci. 99 (2002) 2760-2765
4. Richardson J.S., and Richardson D.C. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl Acad. Sci. 99 (2002) 2754-2759
5. Broome B.M., and Hecht M.H. Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. J. Mol. Biol. 296 (2000) 961-968
6. Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
7. Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Folding Des. 3 (1998) R9-R23
8. H single domain with a germ-line scaffold. J. Mol. Biol. 337 (2004) 893-903
9. Ewert S., Huber T., Honegger A., and Pluckthun A. Biophysical properties of human antibody variable domains. J. Mol. Biol. 325 (2003) 531-553
10. Jespers L., Schon O., Famm K., and Winter G. Aggregation-resistant domain antibodies selected on phage by heat denaturation. Nat. Biotechnol. 22 (2004) 1161-1165
11. Famm K., and Winter G. Engineering aggregation-resistant proteins by directed evolution. Protein Eng. Des. Sel. 20 (2006) 413-416
12. Ewert S., Cambillau C., Conrath K., and Pluckthun A. Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains. Biochemistry 41 (2002) 3628-3636
13. Jung S., Honegger A., and Pluckthun A. Selection for improved protein stability by phage display. J. Mol. Biol. 294 (1999) 163-180
14. Khurana R., Gillespie J.R., Talapatra A., Minert L.J., Ionescu-Zanetti C., Millett I., and Fink A.L. Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40 (2001) 3525-3535
15. Pace C.N., and Scholtz J.M. In: Creighton T.E. (Ed). Protein Structure, A Practical Approach. 2nd edit. (1997), Oxford University Press, New York 299-321
16. Itzhaki L.S., Evans P.A., Dobson C.M., and Radford S.E. Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry 33 (1994) 5212-5220
17. Clackson T., Hoogenboom H.R., Griffiths A.D., and Winter G. Making antibody fragments using phage display libraries. Nature 352 (1991) 624-628
18. McCafferty J., Griffiths A.D., Winter G., and Chiswell D.J. Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348 (1990) 552-554
19. Fersht A. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding (1999), W.H. Freeman, New York
20. Kabat E.A., National Institutes of Health (US), and Columbia University. Sequences of Proteins of Immunological Interest. 5th edit. (1991), US Department of Health and Human Services Public Health Service National Institutes of Health, Bethesda, MD NIH publication no. 91-3242
21. H segments with different hypervariable loops. J. Mol. Biol. 227 (1992) 776-798
22. Honegger A., and Pluckthun A. Yet another numbering scheme for immunoglobulin variable domains: an automatic modeling and analysis tool. J. Mol. Biol. 309 (2001) 657-670
23. Martin A.C. Accessing the Kabat antibody sequence database by computer. Proteins: Struct. Funct. Genet. 25 (1996) 130-133