Fluorine substitutions in an antigenic peptide selectively modulate T-cell receptor binding in a minimally perturbing manner

Biochemical Journal

Volumn 423, Issue 3, 2009, Pages 353-361

  Piepenbrink, Kurt H ^a   Borbulevych, Oleg Y ^a   Sommese, Ruth F ^b   Clemens, John ^a   Armstrong, Kathryn M ^a   Desmond, Clare ^a   Do, Priscilla ^a   Baker, Brian M ^a  

^a UNIVERSITY OF NOTRE DAME   (United States)

^b STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Antigenic peptide; Fluorine; Major histocompatibility complex (MHC); T cell receptor (TCR); Thermodynamics; Vaccine design

Indexed keywords

ANTIGENIC PEPTIDE; ANTIGENIC PEPTIDES; BINDING AFFINITIES; BIOPHYSICAL STUDIES; CRYSTALLOGRAPHIC STRUCTURE; DESIGN APPROACHES; FAST KINETICS; FLUORINE SUBSTITUTION; HUMAN T CELLS; IMMUNE RESPONSE; MAJOR HISTOCOMPATIBILITY COMPLEX; MAJOR HISTOCOMPATIBILITY COMPLEX (MHC); T-CELL RECEPTOR (TCR); T-CELL RECEPTORS;

AMINES; BINDING ENERGY; ELECTRIC REACTORS; FLUORINATION; FLUORINE; HALOGENATION; HYDROPHOBICITY; MOLECULAR BIOLOGY; MOLECULAR RECOGNITION; PEPTIDES; TAXATION; THERMAL CONDUCTIVITY OF SOLIDS; THERMODYNAMICS; VACCINES;

CELL MEMBRANES;

FLUORINE; T LYMPHOCYTE RECEPTOR; T LYMPHOCYTE RECEPTOR B7; TAX PEPTIDE; UNCLASSIFIED DRUG;

ANTIGEN BINDING; ANTIGEN RECOGNITION; ARTICLE; BINDING AFFINITY; CHEMICAL STRUCTURE; CHEMISTRY; CONTROLLED STUDY; CRYSTALLOGRAPHY; FLUORINATION; HUMAN T CELL LEUKEMIA VIRUS 1; HYDROPHOBICITY; MOLECULAR RECOGNITION; PRIORITY JOURNAL; PROTEIN STRUCTURE; RECEPTOR BINDING; SUBSTITUTION REACTION; THERMODYNAMICS;

FLUORINE; GENE PRODUCTS, TAX; HLA ANTIGENS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; PEPTIDES; PROTEIN BINDING; RECEPTORS, ANTIGEN, T-CELL; VIRAL VACCINES;

HUMAN T-LYMPHOTROPIC VIRUS 1;

EID: 70350094712     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090732     Document Type: Article

References (22)

1. Holler, P. D., Holman, P. O., Shusta, E. V., O'Herrin, S., Wittrup, K. D. and Kranz, D. M. (2000) In vitro evolution of a T cell receptor with high affinity for peptide/MHC. Proc. Natl. Acad. Sci. U.S.A. 97, 5387-5392
2. Li, Y., Moysey, R., Molloy, P. E., Vuidepot, A.-L., Mahon, T., Baston, E., Dunn, S., Liddy, N., Jacob, J., Jakobsen, B. K. and Boulter, J. M. (2005) Directed evolution of human T-cell receptors with picomolar affinities by phage display. Nat. Biotech. 23, 349-354
3. Haidar, J. N., Pierce, B., Yu, Y., Tong, W., Li, M. and Weng, Z. (2009) Structure-based design of a T-cell receptor leads to nearly 100-fold improvement in binding affinity for pepMHC. Proteins 74, 948-960
4. Slansky, J. E., Rattis, F. M., Boyd, L. F., Fahmy, T., Jaffee, E. M., Schneck, J. P., Margulies, D. H. and Pardoll, D. M. (2000) Enhanced antigen-specific antitumor immunity with altered peptide ligands that stabilize the MHC-peptide-TCR complex. Immunity 13, 529-538
5. McMahan, R. H. and Slansky, J. E. (2007) Mobilizing the low-avidity T cell repertoire to kill tumors. Semin. Cancer Biol. 17, 317-329
6. Muller, K., Faeh, C. and Diederich, F. (2007) Fluorine in pharmaceuticals: looking beyond intuition. Science 317, 1881-1886
7. Gomez-Nunez, M., Haro, K. J., Dao, T., Chau, D., Won, A., Escobar-Alvarez, S., Zakhaleva, V., Korontsvit, T., Gin, D. Y. and Scheinberg, D. A. (2008) Non-natural and photo-reactive amino acids as biochemical probes of immune function. PLoS ONE 3, e3938
8. Utz, U., Banks, D., Jacobson, S. and Biddison, W. E. (1996) Analysis of the T-cell receptor repertoire of human T-cell leukemia virus type 1 (HTLV-1) Tax-specific CD8+ cytotoxic T lymphocytes from patients with HTLV-1-associated disease: evidence for oligoclonal expansion. J. Virol. 70, 843-851
9. Ding, Y. H., Smith, K. J., Garboczi, D. N., Utz, U., Biddison, W. E. and Wiley, D. C. (1998) Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 8, 403-411
10. Davis-Harrison, R. L., Armstrong, K. M. and Baker, B. M. (2005) Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/MHC ligand. J. Mol. Biol. 346, 533-550
11. Biffinger, J. C., Kim, H. W. and DiMagno, S. G. (2004) The polar hydrophobicity of fluorinated compounds. ChemBioChem. 5, 622-627
12. Bevington, P. R. and Robinson, D. K. (1992) Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, New York
13. Armstrong, K. M. and Baker, B. M. (2007) A comprehensive calorimetric investigation of an entropically driven T Cell receptor-peptide/major histocompatibility complex interaction. Biophys. J. 93, 597-609
14. Gagnon, S. J., Borbulevych, O. Y., Davis-Harrison, R. L., Turner, R. V., Damirjian, M., Wojnarowicz, A., Biddison, W. E. and Baker, B. M. (2006) T cell receptor recognition via cooperative conformational plasticity. J. Mol. Biol. 363, 228-243
15. Garboczi, D. N., Ghosh, P., Utz, U., Fan, Q. R., Biddison, W. E. and Wiley, D. C. (1996) Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141
16. Ding, Y. H., Baker, B. M., Garboczi, D. N., Biddison, W. E. and Wiley, D. C. (1999) Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity 11, 45-56
17. Armstrong, K. M., Piepenbrink, K. H. and Baker, B. M. (2008) Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Biochem. J. 415, 183-196
18. Baker, B. M., Gagnon, S. J., Biddison, W. E. and Wiley, D. C. (2000) Conversion of a T cell antagonist into an agonist by repairing a defect in the TCR/peptide/MHC interface: implications for TCR signaling. Immunity 13, 475-484
19. Dunitz, J. D. (2004) Organic fluorine: odd man out. ChemBioChem 5, 614-621
20. Dunitz, J. D. and Taylor, R. (1997) Organic fluorine hardly ever accepts hydrogen bonds. Chemistry 3, 89-98
21. Howard, J. A. K., Hoy, V. J., O'Hagan, D. and Smith, G. T. (1996) How good is fluorine as a hydrogen bond acceptor? Tetrahedron 52, 12613-12622
22. Sharp, K. A. and Madan, B. (1997) Hydrophobic effect, water structure, and heat capacity changes. J. Phys. Chem. B. 101, 4343-4348