Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Jul 15;90(14):6385–6389. doi: 10.1073/pnas.90.14.6385

Direct selection of antibodies that coordinate metals from semisynthetic combinatorial libraries.

C F Barbas 3rd 1, J S Rosenblum 1, R A Lerner 1
PMCID: PMC46936  PMID: 8341642

Abstract

An iterative strategy for the selection of catalytic metalloantibodies is described. The first stage of this strategy is validated by the selection of semisynthetic antibodies that coordinate a variety of different metal ions and the metal oxide magnetite. These results have implications not only for the development of catalytic metalloantibodies but also for the development of reagents for magnetic resonance imaging, delivery of radioisotopes, and purification of recombinant proteins.

Full text

PDF
6385

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adman E. T. Copper protein structures. Adv Protein Chem. 1991;42:145–197. doi: 10.1016/s0065-3233(08)60536-7. [DOI] [PubMed] [Google Scholar]
  2. Baker B. L., Hultquist D. E. A copper-binding immunoglobulin from a myeloma patient. Studies of the copper-binding site. J Biol Chem. 1978 Dec 10;253(23):8444–8451. [PubMed] [Google Scholar]
  3. Barbas C. F., 3rd, Bain J. D., Hoekstra D. M., Lerner R. A. Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4457–4461. doi: 10.1073/pnas.89.10.4457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Barbas C. F., 3rd, Kang A. S., Lerner R. A., Benkovic S. J. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):7978–7982. doi: 10.1073/pnas.88.18.7978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Brown R. S., Hingerty B. E., Dewan J. C., Klug A. Pb(II)-catalysed cleavage of the sugar-phosphate backbone of yeast tRNAPhe--implications for lead toxicity and self-splicing RNA. Nature. 1983 Jun 9;303(5917):543–546. doi: 10.1038/303543a0. [DOI] [PubMed] [Google Scholar]
  6. Brown S. Engineered iron oxide-adhesion mutants of the Escherichia coli phage lambda receptor. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8651–8655. doi: 10.1073/pnas.89.18.8651. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Chiou S. H. DNA- and protein-scission activities of ascorbate in the presence of copper ion and a copper-peptide complex. J Biochem. 1983 Oct;94(4):1259–1267. doi: 10.1093/oxfordjournals.jbchem.a134471. [DOI] [PubMed] [Google Scholar]
  8. Chothia C., Lesk A. M. Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol. 1987 Aug 20;196(4):901–917. doi: 10.1016/0022-2836(87)90412-8. [DOI] [PubMed] [Google Scholar]
  9. Crispino G. A., Ho P. T., Sharpless K. B. Selective perhydroxylation of squalene: taming the arithmetic demon. Science. 1993 Jan 1;259(5091):64–66. doi: 10.1126/science.8418495. [DOI] [PubMed] [Google Scholar]
  10. Higaki J. N., Haymore B. L., Chen S., Fletterick R. J., Craik C. S. Regulation of serine protease activity by an engineered metal switch. Biochemistry. 1990 Sep 18;29(37):8582–8586. doi: 10.1021/bi00489a012. [DOI] [PubMed] [Google Scholar]
  11. Howard J. B., Rees D. C. Perspectives on non-heme iron protein chemistry. Adv Protein Chem. 1991;42:199–280. doi: 10.1016/s0065-3233(08)60537-9. [DOI] [PubMed] [Google Scholar]
  12. Iverson B. L., Iverson S. A., Roberts V. A., Getzoff E. D., Tainer J. A., Benkovic S. J., Lerner R. A. Metalloantibodies. Science. 1990 Aug 10;249(4969):659–662. doi: 10.1126/science.2116666. [DOI] [PubMed] [Google Scholar]
  13. Matsunaga T. Applications of bacterial magnets. Trends Biotechnol. 1991 Mar;9(3):91–95. doi: 10.1016/0167-7799(91)90031-c. [DOI] [PubMed] [Google Scholar]
  14. Meldrum F. C., Heywood B. R., Mann S. Magnetoferritin: in vitro synthesis of a novel magnetic protein. Science. 1992 Jul 24;257(5069):522–523. doi: 10.1126/science.1636086. [DOI] [PubMed] [Google Scholar]
  15. Noyori R. Chiral metal complexes as discriminating molecular catalysts. Science. 1990 Jun 8;248(4960):1194–1199. doi: 10.1126/science.248.4960.1194. [DOI] [PubMed] [Google Scholar]
  16. Roberts V. A., Iverson B. L., Iverson S. A., Benkovic S. J., Lerner R. A., Getzoff E. D., Tainer J. A. Antibody remodeling: a general solution to the design of a metal-coordination site in an antibody binding pocket. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6654–6658. doi: 10.1073/pnas.87.17.6654. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tainer J. A., Roberts V. A., Getzoff E. D. Metal-binding sites in proteins. Curr Opin Biotechnol. 1991 Aug;2(4):582–591. doi: 10.1016/0958-1669(91)90084-i. [DOI] [PubMed] [Google Scholar]
  18. Toma S., Campagnoli S., Margarit I., Gianna R., Grandi G., Bolognesi M., De Filippis V., Fontana A. Grafting of a calcium-binding loop of thermolysin to Bacillus subtilis neutral protease. Biochemistry. 1991 Jan 8;30(1):97–106. doi: 10.1021/bi00215a015. [DOI] [PubMed] [Google Scholar]
  19. Vallee B. L., Auld D. S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry. 1990 Jun 19;29(24):5647–5659. doi: 10.1021/bi00476a001. [DOI] [PubMed] [Google Scholar]
  20. Wylie D. E., Lu D., Carlson L. D., Carlson R., Babacan K. F., Schuster S. M., Wagner F. W. Monoclonal antibodies specific for mercuric ions. Proc Natl Acad Sci U S A. 1992 May 1;89(9):4104–4108. doi: 10.1073/pnas.89.9.4104. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES