Surface plasmon resonance characterization of specific binding of polyglutamine aggregation inhibitors to the expanded polyglutamine stretch

Biochemical and Biophysical Research Communications

Volumn 378, Issue 3, 2009, Pages 634-639

  Okamoto, Yuma ^a,b   Nagai, Yoshitaka ^b   Fujikake, Nobuhiro ^b   Akiko Popiel, H ^b   Yoshioka, Tohru ^c   Toda, Tatsushi ^b   Inui, Takashi ^a  

^a Osaka Prefecture University   (Japan)

^b OSAKA UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^c KAOHSIUNG MEDICAL UNIVERSITY   (Taiwan)

Author keywords

Aggregation; Inhibitor; Neurodegeneration; Peptide; Polyglutamine; Surface plasmon resonance

Indexed keywords

BINDING PROTEIN; CONGO RED; POLYGLUTAMINE; PROTEIN POLYGLUTAMINE BINDING PEPTIDE 1; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; SURFACE PLASMON RESONANCE;

AMINO ACID SEQUENCE; DRUG EVALUATION, PRECLINICAL; HUMANS; MOLECULAR SEQUENCE DATA; NEURODEGENERATIVE DISEASES; OLIGOPEPTIDES; PEPTIDES; PROTEIN BINDING; SURFACE PLASMON RESONANCE;

EID: 57749186661     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2008.11.094     Document Type: Article

References (31)

1. Orr H.T., and Zoghbi H.Y. Trinucleotide repeat disorders. Annu. Rev. Neurosci. 30 (2007) 575-621
2. Shao J., and Diamond M.I. Polyglutamine diseases: emerging concepts in pathogenesis and therapy. Hum. Mol. Genet. 16 Spec. No. 2 (2007) R115-R123
3. Ross C.A., and Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 10 Suppl. (2004) S10-S17
4. Y. Nagai, H.A. Popiel, Conformational changes and aggregation of expanded polyglutamine proteins as therapeutic targets of the polyglutamine diseases: exposed β-sheet hypothesis, Curr. Pharm. Des., in press.
5. Nagai Y., Tucker T., Ren H., et al. Inhibition of polyglutamine protein aggregation and cell death by novel peptides identified by phage display screening. J. Biol. Chem. 275 (2000) 10437-10442
6. Nagai Y., Inui T., Popiel H.A., et al. A toxic monomeric conformer of the polyglutamine protein. Nat. Struct. Mol. Biol. 14 (2007) 332-340
7. Takahashi Y., Okamoto Y., Popiel H.A., et al. Detection of polyglutamine protein oligomers in cells by fluorescence correlation spectroscopy. J. Biol. Chem. 282 (2007) 24039-24048
8. Nagai Y., Fujikake N., Ohno K., et al. Prevention of polyglutamine oligomerization and neurodegeneration by the peptide inhibitor QBP1 in Drosophila. Hum. Mol. Genet. 12 (2003) 1253-1259
9. Popiel H.A., Nagai Y., Fujikake N., et al. Protein transduction domain-mediated delivery of QBP1 suppresses polyglutamine-induced neurodegeneration in vivo. Mol. Ther. 15 (2007) 303-309
10. Popiel H.A., Nagai Y., Fujikake N., et al. Delivery of the aggregate inhibitor peptide QBP1 into the mouse brain using PTDs and its therapeutic effect on polyglutamine disease mice. Neurosci. Lett. 449 (2009) 87-92
11. Heiser V., Scherzinger E., Boeddrich A., et al. Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy. Proc. Natl. Acad. Sci. USA 97 (2000) 6739-6744
12. Heiser V., Engemann S., Brocker W., et al. Identification of benzothiazoles as potential polyglutamine aggregation inhibitors of Huntington's disease by using an automated filter retardation assay. Proc. Natl. Acad. Sci. USA 99 Suppl. 4 (2002) 16400-16406
13. McGovern S.L., Caselli E., Grigorieff N., et al. A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J. Med. Chem. 45 (2002) 1712-1722
14. Feng B.Y., Toyama B.H., Wille H., et al. Small-molecule aggregates inhibit amyloid polymerization. Nat. Chem. Biol. 4 (2008) 197-199
15. Ren H., Nagai Y., Tucker T., et al. Amino acid sequence requirements of peptides that inhibit polyglutamine-protein aggregation and cell death. Biochem. Biophys. Res. Commun. 288 (2001) 703-710
16. Giannetti A.M., Koch B.D., and Browner M.F. Surface plasmon resonance based assay for the detection and characterization of promiscuous inhibitors. J. Med. Chem. 51 (2008) 574-580
17. Frid P., Anisimov S.V., and Popovic N. Congo red and protein aggregation in neurodegenerative diseases. Brain Res. Rev. 53 (2007) 135-160
18. LeVine III H. Quantification of β-sheet amyloid fibril structures with thioflavin T. Methods Enzymol. 309 (1999) 274-284
19. Poirier M.A., Li H., Macosko J., et al. Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. 277 (2002) 41032-41037
20. Rishton G.M. Nonleadlikeness and leadlikeness in biochemical screening. Drug Discov. Today 8 (2003) 86-96
21. Wood N.I., Pallier P.N., Wanderer J., et al. Systemic administration of Congo red does not improve motor or cognitive function in R6/2 mice. Neurobiol. Dis. 25 (2007) 342-353
22. Hockly E., Tse J., Barker A.L., et al. Evaluation of the benzothiazole aggregation inhibitors riluzole and PGL-135 as therapeutics for Huntington's disease. Neurobiol. Dis. 21 (2006) 228-236
23. Sanchez I., Mahlke C., and Yuan J. Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421 (2003) 373-379
24. Huber W. A new strategy for improved secondary screening and lead optimization using high-resolution SPR characterization of compound-target interactions. J. Mol. Recognit. 18 (2005) 273-281
25. Kawatake S., Nishimura Y., Sakaguchi S., et al. Surface plasmon resonance analysis for the screening of anti-prion compounds. Biol. Pharm. Bull. 29 (2006) 927-932
26. Cairo C.W., Strzelec A., Murphy R.M., et al. Affinity-based inhibition of β-amyloid toxicity. Biochemistry (Mosc.) 41 (2002) 8620-8629
27. Trottier Y., Lutz Y., Stevanin G., et al. Polyglutamine expansion as a pathological epitope in Huntington's disease and four dominant cerebellar ataxias. Nature 378 (1995) 403-406
28. Peters-Libeu C., Newhouse Y., Krishnan P., et al. Crystallization and diffraction properties of the Fab fragment of 3B5H10, an antibody specific for disease-causing polyglutamine stretches. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 61 (2005) 1065-1068
29. Ko J., Ou S., and Patterson P.H. New anti-huntingtin monoclonal antibodies: implications for huntingtin conformation and its binding proteins. Brain Res. Bull. 56 (2001) 319-329
30. Klein F.A., Pastore A., Masino L., et al. Pathogenic and non-pathogenic polyglutamine tracts have similar structural properties: towards a length-dependent toxicity gradient. J. Mol. Biol. 371 (2007) 235-244
31. Li P., Huey-Tubman K.E., Gao T., et al. The structure of a polyQ-anti-polyQ complex reveals binding according to a linear lattice model. Nat. Struct. Mol. Biol. 14 (2007) 381-387