Designed hydrophilic and charge mutations of the fibronectin domain: Towards tailored protein biodistribution

Protein Engineering, Design and Selection

Volumn 25, Issue 10, 2012, Pages 639-647

  Hackel, Benjamin J ^a   Sathirachinda, Ataya ^a   Gambhir, Sanjiv S ^b  

^a STANFORD UNIVERSITY   (United States)

^b Stanford University   (United States)

Author keywords

biodistribution; charge; fibronectin; hydrophilicity; protein engineering

Indexed keywords

BACKGROUND SIGNALS; BINDING SPECIFICITIES; BIODISTRIBUTIONS; CHARGE; FIBRONECTIN; FIBRONECTIN DOMAINS; HUMAN FIBRONECTIN; MODEL PROTEINS; PEARSON'S CORRELATION COEFFICIENTS; PHYLOGENETIC ANALYSIS; PROTEIN ENGINEERING;

CLONING; CORRELATION METHODS; DRUG DELIVERY; HYDROPHILICITY; MAMMALS; MOLECULAR IMAGING; POSITRON EMISSION TOMOGRAPHY; PROTEINS;

SCAFFOLDS (BIOLOGY);

AMINO ACID DERIVATIVE; COPPER 64; FIBRONECTIN; SCAFFOLD PROTEIN;

ACIDITY; ALKALINITY; ANIMAL CELL; ANIMAL MODEL; ARTICLE; DRUG LIVER LEVEL; DRUG UPTAKE; FEMALE; GENE MUTATION; HUMAN; HUMAN CELL; HYDROPHILICITY; KIDNEY TUBULE ABSORPTION; MOLECULAR CLONING; MOLECULAR IMAGING; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYLOGENETIC TREE; POSITRON EMISSION TOMOGRAPHY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; SQUAMOUS CELL CARCINOMA;

ANIMALS; CELL LINE; FIBRONECTINS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICE; MICE, NUDE; MODELS, MOLECULAR; MUTATION; PHYLOGENY; POSITRON-EMISSION TOMOGRAPHY; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECEPTOR, EPIDERMAL GROWTH FACTOR; RECOMBINANT PROTEINS; TISSUE DISTRIBUTION;

MUS;

EID: 84866984245     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzs036     Document Type: Article

References (34)

1. Birtalan, S., Fisher, R.D. and Sidhu, S.S. (2010) Mol. Biosyst., 6, 1186-1194.
2. Carver, R.S., Stevenson, M.C., Scheving, L.A. and Russell, W.E. (2002) Gastroenterology, 123, 2017-2027.
3. Dickinson, C.D., Veerapandian, B., Dai, X.P., Hamlin, R.C., Xuong, N.H., Ruoslahti, E. and Ely, K.R. (1994) J. Mol. Biol., 236, 1079-1092.
4. Fraczkiewicz, R. and Braun, W. (1998) J. Comput. Chem., 19, 319-333.
5. Gainkam, L.O.T., Huang, L., Caveliers, V., et al. (2008) J. Nucl. Med., 49, 788-795.
6. García Garayoa, E., Schweinsberg, C., Maes, V., Brans, L., Bläuenstein, P., Tourwe, D.A., Schibli, R. and Schubiger, P.A. (2008) Bioconjug. Chem., 19, 2409-2416.
7. Giglio, J., Fernández, S., Rey, A. and Cerecetto, H. (2011) Bioorg. Med. Chem. Lett., 21, 394-397.
8. Gilbreth, R.N., Esaki, K., Koide, A., Sidhu, S.S. and Koide, S. (2008) J. Mol. Biol., 381, 407-418.
9. Glaser, M., Morrison, M., Solbakken, M., Arukwe, J., Karlsen, H., Wiggen, U., Champion, S., Kindberg, G.M. and Cuthbertson, A. (2008) Bioconjug. Chem., 19, 951-957.
10. Hackel, B.J., Ackerman, M.E., Howland, S.W. and Wittrup, K.D. (2010) J. Mol. Biol., 401, 84-96.
11. Hackel, B.J., Kapila, A. and Wittrup, K.D. (2008) J. Mol. Biol., 381, 1238-1252.
12. Hackel, B.J., Kimura, R.H. and Gambhir, S.S. (2012) Radiology, 263, 179-188.
13. Huang, J., Koide, A., Makabe, K. and Koide, S. (2008a) Proc. Natl. Acad. Sci. USA, 105, 6578-6583.
14. Huang, L., Gainkam, L.O.T., Caveliers, V., Vanhove, C., Keyaerts, M., De Baetselier, P., Bossuyt, A., Revets, H. and Lahoutte, T. (2008b) Mol. ImagingBiol., 10, 167-175.
15. Huang, J., Makabe, K., Biancalana, M., Koide, A. and Koide, S. (2009) J. Mol. Biol., 392, 1221-1231.
16. Jiang, L., Kimura, R.H., Miao, Z., et al. (2010) J. Nucl. Med., 51, 251-258.
17. Kimura, R.H., Teed, R., Hackel, B.J., Pysz, M.A., Chuang, C.Z., Sathirachinda, A., Willmann, J.K. and Gambhir, S.S. (2012) Clin. Cancer Res., 18, 839-849.
18. Koehler, L., Graf, F., Bergmann, R., Steinbach, J., Pietzsch, J. and Wuest, F. (2010) Eur J Med Chem, 45, 727-737.
19. Koide, A., Abbatiello, S., Rothgery, L. and Koide, S. (2002) Proc. Natl. Acad. Sci. USA, 99, 1253-1258.
20. Koide, A., Gilbreth, R.N., Esaki, K., Tereshko, V. and Koide, S. (2007) Proc. Natl. Acad. Sci. USA, 104, 6632-6637.
21. Kunstler, J.-U., Seidel, G., Bergmann, R., et al. (2010) Eur. J. Med. Chem., 45, 3645-3655.
22. Kyte, J. and Doolittle, R.F. (1982) J. Mol. Biol., 157, 105-132.
23. Lipovsek, D. (2011) Protein Eng. Des Sel., 24, 3-9.
24. Main, A.L., Harvey, T.S., Baron, M., Boyd, J. and Campbell, I.D. (1992) Cell, 71, 671-678.
25. Miao, Z., Levi, J. and Cheng, Z. (2010) Amino acids, 41, 1037-1047.
26. Ono, M., Arano, Y., Mukai, T., Saga, T., Fujioka, Y., Ogawa, K., Kawashima, H., Konishi, J. and Saji, H. (2002) Bioconjug. Chem., 13, 491-501.
27. Pimm, M.V., Gribben, S.J., Bogdan, K. and Hudecz, F. (1995) J. Control. Release, 37, 161-172.
28. Ren, G., Zhang, R., Liu, Z., Webster, J.M., Miao, Z., Gambhir, S.S., Syud, F.A. and Cheng, Z. (2009) J. Nucl. Med., 50, 1492-1499.
29. Schottelius, M., Wester, H.-J., Reubi, J.C., Senekowitsch-Schmidtke, R. and Schwaiger, M. (2002) Bioconjug. Chem., 13, 1021-1030.
30. Tolmachev, V., Friedman, M., Sandström, M., Eriksson, T.L.J., Rosik, D., Hodik, M., Sta°hl, S., Frejd, F.Y. and Orlova, A. (2009) J. Nucl. Med., 50, 274-283.
31. Tran, T., Engfeldt, T., Orlova, A., Sandström, M., Feldwisch, J., Abrahmsén, L., Wennborg, A., Tolmachev, V. and Karlström, A.E. (2007) Bioconjug. Chem., 18, 1956-1964.
32. Tran, T.A., Ekblad, T., Orlova, A., Sandström, M., Feldwisch, J., Wennborg, A., Abrahmsén, L., Tolmachev, V. and Eriksson Karlström, A. (2008) Bioconjug. Chem., 19, 2568-2576.
33. Wojcik, J., Hantschel, O., Grebien, F., et al. (2010) Nat. Struct. Mol. Biol., 17, 519-527.
34. Zahnd, C., Kawe, M., Stumpp, M.T., et al. (2010) Cancer Res., 70, 1595-1605.