Effective and specific inhibition of the CD40-CD154 costimulatory interaction by a naphthalenesulphonic acid derivative

Chemical Biology and Drug Design

Volumn 76, Issue 4, 2010, Pages 305-313

  Margolles Clark, Emilio ^a   Kenyon, Norma S ^a   Ricordi, Camillo ^a   Buchwald, Peter ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

Author keywords

BAFF; CD40L; costimulatory blockade; immune suppression; OX40; protein protein interaction; THP 1 cells

Indexed keywords

B CELL ACTIVATING FACTOR; CD40 ANTIGEN; CD40 LIGAND; NAPHTHALENESULFONIC ACID DERIVATIVE; OSTEOCLAST DIFFERENTIATION FACTOR; OX40 LIGAND; TUMOR NECROSIS FACTOR ALPHA;

ARTICLE; BONE MARROW CELL; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG STRUCTURE; FLOW CYTOMETRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; HUMAN CELL; IC 50; IMMUNOMODULATION; MASS SPECTROMETRY; MOLECULAR DOCKING; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION;

ANTIGENS, CD40; AZO COMPOUNDS; BINDING SITES; CD40 LIGAND; CELL LINE; COMPUTER SIMULATION; HUMANS; KINETICS; NAPHTHALENESULFONATES; PROTEIN BINDING; TUMOR NECROSIS FACTORS;

EID: 77956400879     PISSN: 17470277     EISSN: 17470285     Source Type: Journal    
DOI: 10.1111/j.1747-0285.2010.01014.x     Document Type: Article

References (37)

1. Vincenti F., Luggen M. (2007) T cell costimulation: a rational target in the therapeutic armamentarium for autoimmune diseases and transplantation. Annu Rev Med 58 : 347 358.
2. Weaver T.A., Charafeddine A.H., Kirk A.D. (2008) Costimulation blockade: towards clinical application. Front Biosci 13 : 2120 2139.
3. Li X.C., Rothstein D.M., Sayegh M.H. (2009) Costimulatory pathways in transplantation: challenges and new developments. Immunol Rev 229 : 271 293.
4. Quezada S.A., Jarvinen L.Z., Lind E.F., Noelle R.J. (2004) CD40/CD154 interactions at the interface of tolerance and immunity. Annu Rev Immunol 22 : 307 328.
5. Elgueta R., Benson M.J., de Vries V.C., Wasiuk A., Guo Y., Noelle R.J. (2009) Molecular mechanism and function of CD40/CD40L engagement in the immune system. Immunol Rev 229 : 152 172.
6. Kenyon N.S., Chatzipetrou M., Masetti M., Ranuncoli A., Oliveira M., Wagner J.L., Kirk A.D., Harlan D.M., Burkly L.C., Ricordi C. (1999) Long-term survival and function of intrahepatic islet allografts in rhesus monkeys treated with humanized anti-CD154. Proc Natl Acad Sci USA 96 : 8132 8137. (Pubitemid 29328420)
7. Cardona K., Korbutt G.S., Milas Z., Lyon J., Cano J., Jiang W., Bello-Laborn H., Hacquoil B., Strobert E., Gangappa S., Weber C.J., Pearson T.C., Rajotte R.V., Larsen C.P. (2006) Long-term survival of neonatal porcine islets in nonhuman primates by targeting costimulation pathways. Nat Med 12 : 304 306.
8. Wagner D.H. Jr., Vaitaitis G., Sanderson R., Poulin M., Dobbs C., Haskins K. (2002) Expression of CD40 identifies a unique pathogenic T cell population in type 1 diabetes. Proc Natl Acad Sci USA 99 : 3782 3787.
9. Bour-Jordan H., Salomon B.L., Thompson H.L., Szot G.L., Bernhard M.R., Bluestone J.A. (2004) Costimulation controls diabetes by altering the balance of pathogenic and regulatory T cells. J Clin Invest 114 : 979 987.
10. Margolles-Clark E., Jacques-Silva M.C., Ganesan L., Umland O., Kenyon N.S., Ricordi C., Berggren P.-O., Buchwald P. (2009) Suramin inhibits the CD40-CD154 costimulatory interaction: a possible mechanism for immunosuppressive effects. Biochem Pharmacol 77 : 1236 1245.
11. Margolles-Clark E., Umland O., Kenyon N.S., Ricordi C., Buchwald P. (2009) Small molecule costimulatory blockade: organic dye inhibitors of the CD40-CD154 interaction. J Mol Med 87 : 1133 1143.
12. Buchwald P., Margolles-Clark E., Kenyon N.S., Ricordi C. (2010) Organic dyes as small molecule protein-protein interaction inhibitors for the CD40-CD154 costimulatory interaction. J Mol Recognit 23 : 65 73.
13. Arkin M.R., Wells J.A. (2004) Small-molecule inhibitors of protein-protein interactions: progressing towards the dream. Nat Rev Drug Discov 3 : 301 317.
14. Wells J.A., McClendon C.L. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450 : 1001 1009.
15. Higueruelo A.P., Schreyer A., Bickerton G.R., Pitt W.R., Groom C.R., Blundell T.L. (2009) Atomic interactions and profile of small molecules disrupting protein-protein interfaces: the TIMBAL database. Chem Biol Drug Des 74 : 457 467.
16. Morris G.M., Goodsell D.S., Halliday R.S., Huey R., Hart W.E., Belew R.K., Olson A.J. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19 : 1639 1662.
17. Karpusas M., Lucci J., Ferrant J., Benjamin C., Taylor F.R., Strauch K., Garber E., Hsu Y.M. (2001) Structure of CD40 ligand in complex with the Fab fragment of a neutralizing humanized antibody. Structure 9 : 321 329.
18. Gordon N.C., Pan B., Hymowitz S.G., Yin J., Kelley R.F., Cochran A.G., Yan M., Dixit V.M., Fairbrother W.J., Starovasnik M.A. (2003) BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site. Biochemistry 42 : 5977 5983.
19. Sanchez A.M., Barra M., de Rossi R.H. (1999) On the mechanism of the acid/base-catalyzed thermal cis-trans isomerization of methyl orange. J Org Chem 64 : 1604 1609.
20. Dugave C., Demange L. (2003) Cis-trans isomerization of organic molecules and biomolecules: implications and applications. Chem Rev 103 : 2475 2532.
21. Cella M., Scheidegger D., Palmer-Lehmann K., Lane P., Lanzavecchia A., Alber G. (1996) Ligation of CD40 on dendritic cells triggers production of high levels of interleukin-12 and enhances T cell stimulatory capacity: T-T help via APC activation. J Exp Med 184 : 747 752.
22. Aldinucci D., Poletto D., Nanni P., Degan M., Rupolo M., Pinto A., Gattei V. (2002) CD40L induces proliferation, self-renewal, rescue from apoptosis, and production of cytokines by CD40-expressing AML blasts. Exp Hematol 30 : 1283 1292.
23. Fuller J.C., Burgoyne N.J., Jackson R.M. (2009) Predicting druggable binding sites at the protein-protein interface. Drug Discov Today 14 : 155 161.
24. Tolliday N., Clemons P.A., Ferraiolo P., Koehler A.N., Lewis T.A., Li X., Schreiber S.L., Gerhard D.S., Eliasof S. (2006) Small molecules, big players: the National Cancer Institute's Initiative for Chemical Genetics. Cancer Res 66 : 8935 8942.
25. Neugebauer A., Hartmann R.W., Klein C.D. (2007) Prediction of protein-protein interaction inhibitors by chemoinformatics and machine learning methods. J Med Chem 50 : 4665 4668.
26. Sperandio O., Reynès C.H., Camproux A.C., Villoutreix B.O. (2010) Rationalizing the chemical space of protein-protein interaction inhibitors. Drug Discov Today 15 : 220 229.
27. Reynès C., Host H., Camproux A.C., Laconde G., Leroux F., Mazars A., Deprez B., Fahraeus R., Villoutreix B.O., Sperandio O. (2010) Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods. PLoS Comput Biol 6 : e1000695.
28. Hopkins A.L., Groom C.R., Alex A. (2004) Ligand efficiency: a useful metric for lead selection. Drug Discov Today 9 : 430 431.
29. Hajduk P.J. (2006) Fragment-based drug design: how big is too big? J Med Chem 49 : 6972 6976.
30. Reynolds C.H., Bembenek S.D., Tounge B.A. (2007) The role of molecular size in ligand efficiency. Bioorg Med Chem Lett 17 : 4258 4261.
31. Buchwald P. (2008) Glucocorticoid receptor binding: a biphasic dependence on molecular size as revealed by the bilinear LinBiExp model. Steroids 73 : 193 208.
32. Brinkworth R.I., Fairlie D.P. (1992) Non-peptidic anti-AIDS agents: inhibition of HIV-1 proteinase by disulfonates. Biochem Biophys Res Commun 188 : 624 630.
33. Rudyk H., Vasiljevic S., Hennion R.M., Birkett C.R., Hope J., Gilbert I.H. (2000) Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells. J Gen Virol 81 (Pt 4 1155 1164.
34. Sousa S.F., Fernandes P.A., Ramos M.J. (2006) Protein-ligand docking: current status and future challenges. Proteins 65 : 15 26.
35. Warren G.L., Andrews C.W., Capelli A.M., Clarke B., LaLonde J., Lambert M.H., Lindvall M., Nevins N., Semus S.F., Senger S., Tedesco G., Wall I.D., Woolven J.M., Peishoff C.E., Head M.S. (2006) A critical assessment of docking programs and scoring functions. J Med Chem 49 : 5912 5931.
36. Bajorath J. (1998) Detailed comparison of two molecular models of the human CD40 ligand with an X-ray structure and critical assessment of model-based mutagenesis and residue mapping studies. J Biol Chem 273 : 24603 24609.
37. Singh J., Garber E., Van Vlijmen H., Karpusas M., Hsu Y.M., Zheng Z., Naismith J.H., Thomas D. (1998) The role of polar interactions in the molecular recognition of CD40L with its receptor CD40. Protein Sci 7 : 1124 1135.