A β-amino acid modified heptapeptide containing a designed recognition element disrupts fibrillization of the amyloid β-peptide

Journal of Peptide Science

Volumn 16, Issue 9, 2010, Pages 443-450

  Castelletto, Valeria ^a   Hamley, Ian W ^a,b   Lim, Teck ^c   De Tullio, Matias B ^d   Castaño, Eduardo M ^d  

^a UNIVERSITY OF READING   (United Kingdom)

^b DIAMOND LIGHT SOURCE LTD   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

^d FUNDACIÓN INSTITUTO LELOIR   (Argentina)

Author keywords

Amyloid; Amyloid beta peptide; Beta amino acid peptide; Fibril

Indexed keywords

AMYLOID BETA PROTEIN[1-42]; BETA AMINO ACID; HEPTAPEPTIDE; LYSYLLEUCYLVALYLPHENYLALANYLPHENYLALANINE; OLIGOMER; THIOFLAVINE; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; NEUROTOXICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN SECONDARY STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY;

AMINO ACID SEQUENCE; AMYLOID; AMYLOID BETA-PEPTIDES; ANIMALS; CIRCULAR DICHROISM; CRYOELECTRON MICROSCOPY; MICROSCOPY, ELECTRON, TRANSMISSION; NEURONS; NEUROTOXINS; OLIGOPEPTIDES; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; RATS; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 77957324485     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1271     Document Type: Article

References (52)

1. Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 2006; 75: 333-366.
2. Hamley IW. Peptide fibrillization. Angew. Chem. Int. Edit. 2007; 46: 8128-8147.
3. Walsh DM, Lomakin A, Benedek GB, Condron MM, Teplow DB. The oligomerization of amyloid β-protein begins intracellularly in cells derived from human brain. J. Biol. Chem. 1997; 272: 22364-22372.
4. Irvine GB, El-Agnaf OMA, Shankar GM, Walsh DM. Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases. Mol. Med. 2008; 14: 451-464.
5. Selkoe DJ. Soluble oligomers of the amyloid beta-protein impair synaptic plasticity and behavior. Behav. Brain Res. 2008; 192: 106-113.
6. Roberson ED, Mucke L. 100 years and counting: prospects for defeating Alzheimer's disease. Science 2006; 314: 781-784. (Pubitemid 44706637)
7. Doig AJ. Peptide inhibitors of beta-amyloid aggregation. Curr. Opin. Drug Discov. 2007; 10: 533-539.
8. Melnikova I. Therapies for Alzheimer's disease. Nat. Rev. Drug Discov. 2007; 6: 341-342.
9. Holtzman DM. Alzheimer's disease - moving towards a vaccine. Nature 2008; 454: 418-420.
10. Findeis MA, Musso GM, Arico-Muendel CC, Benjamin HW, Hundal AM, Lee JJ, Chin J, Kelley M, Wakefield J, Hayward NJ, Molineaux SM.Modified-peptide inhibitors of amyloid beta-peptide polymerization. Biochemistry 1999; 38: 6791-6800.
11. Lowe TL, Strzelec A, Kiessling LL, Murphy RM. Structure-function relationships for inhibitors of beta-amyloid toxicity containing the recognition sequence KLVFF. Biochemistry 2001; 40: 7882-7889. (Pubitemid 32622980)
12. Pallitto MM, Ghanta J, Heinzelman P, Kiessling LL, Murphy RM. Recognition sequence design for peptidyl modulators of β-amyloid aggregation and toxicity. Biochemistry 1999; 38: 3570-3578. (Pubitemid 29149475)
13. Gibson TJ, Murphy RM. Design of peptidyl compounds that affect beta-amyloid aggregation: importance of surface tension and contex. Biochemistry 2005; 44: 8898-8907.
14. Gordon DJ, Tappe R, Meredith SC. Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibuits Aβ 1-40 fibrillogenesis. J. Pept. Res. 2002; 60: 37-55.
15. Kokkoni N, Stott K, Amijee H, Mason JM, Doig AJ. N-methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure. Biochemistry 2006; 45: 9906-9918.
16. Austen BM, Paleologou KE, Ali SAE, Qureshi MM, Allsop D, El- Agnaf OMA. Designing peptide inhibitors for oligomerization and toxicity of Alzheimer's beta-amyloid peptide. Biochemistry 2008; 47: 1984-1992.
17. Sato J, Takahashi T, Oshima H, Matsumura S, Mihara H. Design of peptides that form amyloid-like fibrils capturing amyloid beta 1-42 peptides. Chem. Eur. J. 2007; 13: 7745-7752.
18. Madine J, Wang X, Brown DR, Middleton DA. Evaluation of beta-alanine- and GABA-substituted peptides as inhibitors of disease-linked protein aggregation. ChemBioChem 2009; 10: 1982-1987.
19. Matharu B, Gibson G, Parsons R, Huckerby TN, Moore SA, Cooper LJ, Millichamp R, Allsop D, Austen B. Galantamine inhibits beta-amyloid aggregation and cytotoxicity. J. Neurol. Sci. 2009; 280: 49-58.
20. Castelletto V, Hamley IW, Hule RA, Pochan DJ. Helical-ribbon formation by a beta-amino acid modified amyloid beta-peptide fragment. Angew. Chem. Int. Edit. 2009; 48: 2317-2320.
21. Seebach D, Matthews JL. Beta-peptides: a surprise at every turn. Chem. Commun. 1997; 2015-2022.
22. Seebach D, Overhand M, Kuhnle FNM, Martinoni B, Oberer L, Hommel U, Widmer W. Beta-peptides: synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a beta-hexapeptide in solution and its stability towards pepsin. Helv. Chim. Acta 1996; 79: 913-941.
23. Cheng RP, Gellman SH, DeGrado WF. Beta-peptides: from structure to function. Chem. Rev. 2001; 101: 3219-3232.
24. Bose PP, Chatterjee U, Nerelius C, Govender T, Norstrom T, Gogoll A, Sandegren A, Gothelid E, Johansson J, Arvidsson PI. Poly-N-methylated amyloid beta-peptide (A beta) C-terminal fragments reduce a beta toxicity in vitro and in Drosophila melanogaster. J. Med. Chem. 2009; 52: 8002-8009.
25. Anker JN, Hall WP, Lambert MP, Velasco PT, Mrksich M, Klein WL, Van Duyne RP. Detection and identification of bioanalytes with high resolution LSPR spectroscopy and MALDI mass spectrometry. J. Phys. Chem. C 2009; 113: 5891-5894.
26. Chromy BA, Nowak RJ, Lambert MP, Viola KL, Chang L, Velasco PT, Jones BW, Fernandez SJ, Lacor PN, Horowitz P, Finch CE, Krafft GA, Klein WL. Self-assembly of A beta(1-42) into globular neurotoxins. Biochemistry 2003; 42: 12749-12760.
27. Talmon Y. Transmission electron microscopy of complex fluids: the state of the art. Ber Bunsen-Ges. Phys. Chem. 1996; 3: 364-372.
28. Kelly SM, Jess TJ, Price NC. How to study proteins by circular dichroism. Biochim. Biophys. Acta 2005; 1751: 119-139.
29. Laczko I, Vass E, Soos K, Fulop L, Zarandi M, Penke B. Aggregation of Ab(1-42) in the presence of short peptides: conformational studies. J. Pept. Sci. 2008; 14: 731-741.
30. Sian AK, Frears ER, El-Agnaf OMA, Patel BP, Manca MF, Siligardi G, Hussain R, Austen BM. Oligomerization of beta-amyloid of the Alzheimer's and the Dutch-cerebral-haemorrhage types. Biochem. J. 2000; 349: 299-308.
31. Hamley IW, Krysmann MJ, Kelarakis A, Castelletto V, Noirez L, Hule RA, Pochan DJ. Nematic and columnar ordering of a PEG-peptide conjugate in aqueous solution. Chem. Eur. J. 2008; 14: 11369-11375.
32. Krysmann MJ, Castelletto V, Hamley IW. Fibrillisation of hydrophobically modified amyloid peptide fragments in an organic solvent. Soft Matter 2007; 2: 1401-1406. (Pubitemid 47587199)
33. Castelletto V, Hamley IW. Self assembly of a model amphiphilic phenylalanine peptide/polyethylene glycol block copolymer in aqueous solution. Biophys. Chem. 2009; 141: 169-174.
34. Peggion E, Palumbo M, Bonora GM, Toniolo C. Bioorg. Chem. 1974; 3: 125.
35. Gupta M, Bagaria A, Mishra A, Mathur P, Basu A, Ramakumar S, Chauhan VS. Self-assembly of a dipeptide-containing conformationally restricted dehydrophenylalanine residue to form ordered nanotubes. Adv.Mat. 2007; 19: 858.
36. LeVine H. Thiflavine-T interaction with synthetic Alzheimers-disease beta-amyloid peptides - detection of amyloid aggregation in solution. Protein Sci. 1993; 2: 404-410.
37. Nilsson MR. Techniques to study amyloid fibril formation in vitro. Methods 2004; 34: 151-160.
38. Lee E, Huang Z, Ryu J-H, Lee M. Rigid-flexible blockmolecules based on a laterally extended aromatic segment: hierarchical self-assembly into single fibers, flat ribbons and twisted ribbons. Chem. Eur. J. 2008; 14: 6957-6966.
39. Smith AM, Williams RJ, Tang C, Coppo P, Collins RF, Turner ML, Saiani A, Ulijn RV.Fmoc-diphenylalanine self assembles toahydrogel via a novel architecture based on π-π interlocked β-sheets. Adv. Mat. 2008; 20: 37-41.
40. Bohrmann B, Adrian M, Dubochet J, Kuner P, Muller F, Huber W, Nordstedt C, Dobeli H. Self-assembly of beta-amyloid 42 is retarded by small molecular ligands at the stage of structural intermediates. J. Struct. Biol. 2000; 130: 232-246.
41. Krysmann MJ, Castelletto V, Kelarakis A, Hamley IW, Hule RA, Pochan DJ. Self-assembly and hydrogelation of an amyloid peptide fragment. Biochemistry 2008; 47: 4597-4605. (Pubitemid 351555478)
42. Castelletto V, Hamley IW, Harris PJF, Olsson U, Spencer N. Influence of the solvent on the self-assembly of a modified amyloid beta peptide fragment. I. Morphological investigation. J. Phys. Chem. B 2009; 13: 9978-9987.
43. Fezoui Y, Teplow DB. Kinetic studies of amyloid beta-protein fibril assembly - differential effects of alpha-helix stabilization. J. Biol. Chem. 2002; 227: 36948-36954.
44. Wood SJ, Maleeff B, Hart T, Wetzel R. Physical, morphological and functional differences between pH 5.8 and 7.4 aggregates of the Alzheimer's amyloid peptide aβ. J. Mol. Biol. 1996; 256: 870-877.
45. Teplow DB. Structural and kinetic features of amyloid beta-protein fibrillogenesis. Amyloid 1998; 5: 121-142.
46. Caughey B, Lansbury PT. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 2003; 26: 267-269.
47. Lambert MP, Barlow AK, Chromy BA, Edwards C, Freed R, Liosatos M, Morgan TE, Rozovsky I, Trommer B, Viola KL, Wals P, Zhang C, Finch CE, Krafft GA, Klein WL. Diffusible, nonfibrillar ligands derived from A beta(1-42) are potent central nervous system neurotoxins. Proc. Natl. Acad. Sci. U.S.A. 1998; 95: 6448-6453.
48. Bitan G, Kirkitadze MD, Lomakin A, Vollers SS, Benedek GB, Teplow DB. Amyloid beta-protein (A beta) assembly: a beta 40 and A beta 42 oligomerize through distinct pathways. Proc. Natl. Acad. Sci. U.S.A. 2003; 100: 330-335.
49. Bernstein SL, Dupuis NF, Lazo ND, Wyttenbach T, Condron MM, Bitan G, Teplow DB, Shea J-E, Ruotolo BT, Robinson CV, Bowers MT. Amyloid-beta protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease. Nat. Chem. 2009; 1: 326-331.
50. Yu L, Edalji R, Harlan JE, Holzman TF, Lopez AP, Labkovsky B, Hillen H, Barghorn S, Ebert U, Richardson PL, Miesbauer L, Solomon L, Bartley D, Walter K, Johnson RW, Hajduk PJ, Olejniczak ET. Structural characterization of a soluble amyloid beta-peptide oligomer. Biochemistry 2009; 48: 1870-1877.
51. Ward RV, Jennings KH, Jepras R, Neville W, Owen DE, Hawkins J, Christie G, Davis JB, George A, Karran EH, Howlett DR. Fractionation and characterization of oligomeric, protofibrillar and fibrillar forms of beta-amyloid peptide. Biochem. J. 2000; 348: 137-144.
52. Giuffrida ML, Caraci F, Pignataro B, Cataldo S, De Bona P, Bruno V, Molinaro G, Pappalardo G, Messina A, Palmigiano A, Garozzo D, Nicoletti F, Rizzarelli E, Copani A. Beta-amyloid monomers are neuroprotective. J. Neurosci. 2009; 34: 10582-10587.