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Mini Review

D-amino acid-based peptide inhibitors as early or preventative therapy in Alzheimer disease

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Pages 119-124 | Received 10 Dec 2013, Accepted 13 Feb 2014, Published online: 19 Feb 2014

References

  • http://www.alz.org/documents_custom/2013_facts_figures_fact_sheet.pdf.
  • http://www.cdc.gov/nchs/data/databriefs/db116.htm.
  • Hardy JA, Higgins GA. Alzheimer’s disease: the amyloid cascade hypothesis. Science 1992; 256:184 - 5; http://dx.doi.org/10.1126/science.1566067; PMID: 1566067
  • Callaway E. Alzheimer’s drugs take a new tack. Nature 2012; 489:13 - 4; http://dx.doi.org/10.1038/489013a; PMID: 22962697
  • https://investor.lilly.com/releasedetail.cfm?ReleaseID=771353.
  • Miles LA, Crespi GA, Doughty L, Parker MW. Bapineuzumab captures the N-terminus of the Alzheimer’s disease amyloid-beta peptide in a helical conformation. Sci Rep 2013; 3:1302; PMID: 23416764
  • Racke MM, Boone LI, Hepburn DL, Parsadainian M, Bryan MT, Ness DK, Piroozi KS, Jordan WH, Brown DD, Hoffman WP, et al. Exacerbation of cerebral amyloid angiopathy-associated microhemorrhage in amyloid precursor protein transgenic mice by immunotherapy is dependent on antibody recognition of deposited forms of amyloid beta. J Neurosci 2005; 25:629 - 36; http://dx.doi.org/10.1523/JNEUROSCI.4337-04.2005; PMID: 15659599
  • Liu C, Zhao M, Jiang L, Cheng PN, Park J, Sawaya MR, Pensalfini A, Gou D, Berk AJ, Glabe CG, et al. Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates. Proc Natl Acad Sci U S A 2012; 109:20913 - 8; http://dx.doi.org/10.1073/pnas.1218792109; PMID: 23213214
  • Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, et al. Atomic view of a toxic amyloid small oligomer. Science 2012; 335:1228 - 31; http://dx.doi.org/10.1126/science.1213151; PMID: 22403391
  • Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ. Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J Neurosci 1999; 19:8876 - 84; PMID: 10516307
  • Cleary JP, Walsh DM, Hofmeister JJ, Shankar GM, Kuskowski MA, Selkoe DJ, Ashe KH. Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function. Nat Neurosci 2005; 8:79 - 84; http://dx.doi.org/10.1038/nn1372; PMID: 15608634
  • Silveira JR, Raymond GJ, Hughson AG, Race RE, Sim VL, Hayes SF, Caughey B. The most infectious prion protein particles. Nature 2005; 437:257 - 61; http://dx.doi.org/10.1038/nature03989; PMID: 16148934
  • Xue WF, Hellewell AL, Gosal WS, Homans SW, Hewitt EW, Radford SE. Fibril fragmentation enhances amyloid cytotoxicity. J Biol Chem 2009; 284:34272 - 82; http://dx.doi.org/10.1074/jbc.M109.049809; PMID: 19808677
  • Cremades N, Cohen SI, Deas E, Abramov AY, Chen AY, Orte A, Sandal M, Clarke RW, Dunne P, Aprile FA, et al. Direct observation of the interconversion of normal and toxic forms of α-synuclein. Cell 2012; 149:1048 - 59; http://dx.doi.org/10.1016/j.cell.2012.03.037; PMID: 22632969
  • Krishnan R, Goodman JL, Mukhopadhyay S, Pacheco CD, Lemke EA, Deniz AA, Lindquist S. Conserved features of intermediates in amyloid assembly determine their benign or toxic states. Proc Natl Acad Sci U S A 2012; 109:11172 - 7; http://dx.doi.org/10.1073/pnas.1209527109; PMID: 22745165
  • Shahnawaz M, Soto C. Microcin amyloid fibrils A are reservoir of toxic oligomeric species. J Biol Chem 2012; 287:11665 - 76; http://dx.doi.org/10.1074/jbc.M111.282533; PMID: 22337880
  • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyreuther K. Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer’s disease beta A4 peptides. J Mol Biol 1992; 228:460 - 73; http://dx.doi.org/10.1016/0022-2836(92)90835-8; PMID: 1453457
  • Brosig B, Langosch D. The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues. Protein Sci 1998; 7:1052 - 6; http://dx.doi.org/10.1002/pro.5560070423; PMID: 9568912
  • Harmeier A, Wozny C, Rost BR, Munter LM, Hua H, Georgiev O, Beyermann M, Hildebrand PW, Weise C, Schaffner W, et al. Role of amyloid-beta glycine 33 in oligomerization, toxicity, and neuronal plasticity. J Neurosci 2009; 29:7582 - 90; http://dx.doi.org/10.1523/JNEUROSCI.1336-09.2009; PMID: 19515926
  • Sato T, Kienlen-Campard P, Ahmed M, Liu W, Li H, Elliott JI, Aimoto S, Constantinescu SN, Octave JN, Smith SO. Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42. Biochemistry 2006; 45:5503 - 16; http://dx.doi.org/10.1021/bi052485f; PMID: 16634632
  • Balbach JJ, Petkova AT, Oyler NA, Antzutkin ON, Gordon DJ, Meredith SC, Tycko R. Supramolecular structure in full-length Alzheimer’s beta-amyloid fibrils: evidence for a parallel beta-sheet organization from solid-state nuclear magnetic resonance. Biophys J 2002; 83:1205 - 16; http://dx.doi.org/10.1016/S0006-3495(02)75244-2; PMID: 12124300
  • Lührs T, Ritter C, Adrian M, Riek-Loher D, Bohrmann B, Döbeli H, Schubert D, Riek R. 3D structure of Alzheimer’s amyloid-beta(1-42) fibrils. Proc Natl Acad Sci U S A 2005; 102:17342 - 7; http://dx.doi.org/10.1073/pnas.0506723102; PMID: 16293696
  • Fawzi NL, Ying J, Ghirlando R, Torchia DA, Clore GM. Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR. Nature 2011; 480:268 - 72; http://dx.doi.org/10.1038/nature10577; PMID: 22037310
  • Ono K, et al. Exogenous amyloidogenic proteins function as seeds in amyloid β-protein aggregation. Biochimica et Biophysica Acta (BBA) -. Molecular Basis of Disease 2014; 1842:646 - 53; http://dx.doi.org/10.1016/j.bbadis.2014.01.002
  • Zhou N, Luo Z, Luo J, Fan X, Cayabyab M, Hiraoka M, Liu D, Han X, Pesavento J, Dong CZ, et al. Exploring the stereochemistry of CXCR4-peptide recognition and inhibiting HIV-1 entry with D-peptides derived from chemokines. J Biol Chem 2002; 277:17476 - 85; http://dx.doi.org/10.1074/jbc.M202063200; PMID: 11880384
  • Bork K, Yasothan U, Kirkpatrick P. Icatibant. Nat Rev Drug Discov 2008; 7:801 - 2; http://dx.doi.org/10.1038/nrd2694
  • Taylor M, Moore S, Mayes J, Parkin E, Beeg M, Canovi M, Gobbi M, Mann DM, Allsop D. Development of a proteolytically stable retro-inverso peptide inhibitor of beta-amyloid oligomerization as a potential novel treatment for Alzheimer’s disease. Biochemistry 2010; 49:3261 - 72; http://dx.doi.org/10.1021/bi100144m; PMID: 20230062
  • Soto C, Kindy MS, Baumann M, Frangione B. Inhibition of Alzheimer’s amyloidosis by peptides that prevent beta-sheet conformation. Biochem Biophys Res Commun 1996; 226:672 - 80; http://dx.doi.org/10.1006/bbrc.1996.1413; PMID: 8831674
  • Tjernberg LO, Näslund J, Lindqvist F, Johansson J, Karlström AR, Thyberg J, Terenius L, Nordstedt C. Arrest of beta-amyloid fibril formation by a pentapeptide ligand. J Biol Chem 1996; 271:8545 - 8; http://dx.doi.org/10.1074/jbc.271.15.8545; PMID: 8621479
  • Tjernberg LO, Lilliehöök C, Callaway DJ, Näslund J, Hahne S, Thyberg J, Terenius L, Nordstedt C. Controlling amyloid beta-peptide fibril formation with protease-stable ligands. J Biol Chem 1997; 272:12601 - 5; http://dx.doi.org/10.1074/jbc.272.19.12601; PMID: 9139713
  • Findeis MA, Musso GM, Arico-Muendel CC, Benjamin HW, Hundal AM, Lee JJ, Chin J, Kelley M, Wakefield J, Hayward NJ, et al. Modified-peptide inhibitors of amyloid beta-peptide polymerization. Biochemistry 1999; 38:6791 - 800; http://dx.doi.org/10.1021/bi982824n; PMID: 10346900
  • Chalifour RJ, McLaughlin RW, Lavoie L, Morissette C, Tremblay N, Boulé M, Sarazin P, Stéa D, Lacombe D, Tremblay P, et al. Stereoselective interactions of peptide inhibitors with the beta-amyloid peptide. J Biol Chem 2003; 278:34874 - 81; http://dx.doi.org/10.1074/jbc.M212694200; PMID: 12840031
  • Bieschke J, Herbst M, Wiglenda T, Friedrich RP, Boeddrich A, Schiele F, Kleckers D, Lopez del Amo JM, Grüning BA, Wang Q, et al. Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils. Nat Chem Biol 2012; 8:93 - 101; http://dx.doi.org/10.1038/nchembio.719; PMID: 22101602
  • Jiang L, Liu C, Leibly D, Landau M, Zhao M, Hughes MP, Eisenberg DS. Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid beta. Elife 2013; 2:e00857; http://dx.doi.org/10.7554/eLife.00857; PMID: 23878726
  • Wiesehan K, Buder K, Linke RP, Patt S, Stoldt M, Unger E, Schmitt B, Bucci E, Willbold D. Selection of D-amino-acid peptides that bind to Alzheimer’s disease amyloid peptide abeta1-42 by mirror image phage display. Chembiochem 2003; 4:748 - 53; http://dx.doi.org/10.1002/cbic.200300631; PMID: 12898626
  • Wiesehan K, Stöhr J, Nagel-Steger L, van Groen T, Riesner D, Willbold D. Inhibition of cytotoxicity and amyloid fibril formation by a D-amino acid peptide that specifically binds to Alzheimer’s disease amyloid peptide. Protein Eng Des Sel 2008; 21:241 - 6; http://dx.doi.org/10.1093/protein/gzm054; PMID: 18252750
  • van Groen T, Wiesehan K, Funke SA, Kadish I, Nagel-Steger L, Willbold D. Reduction of Alzheimer’s disease amyloid plaque load in transgenic mice by D3, A D-enantiomeric peptide identified by mirror image phage display. ChemMedChem 2008; 3:1848 - 52; http://dx.doi.org/10.1002/cmdc.200800273; PMID: 19016284
  • van Groen T, Kadish I, Wiesehan K, Funke SA, Willbold D. In vitro and in vivo staining characteristics of small, fluorescent, Abeta42-binding D-enantiomeric peptides in transgenic AD mouse models. ChemMedChem 2009; 4:276 - 82; http://dx.doi.org/10.1002/cmdc.200800289; PMID: 19072935
  • Aileen Funke S, van Groen T, Kadish I, Bartnik D, Nagel-Steger L, Brener O, Sehl T, Batra-Safferling R, Moriscot C, Schoehn G, et al. Oral treatment with the d-enantiomeric peptide D3 improves the pathology and behavior of Alzheimer’s Disease transgenic mice. ACS Chem Neurosci 2010; 1:639 - 48; http://dx.doi.org/10.1021/cn100057j; PMID: 22778851
  • 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 - 18; http://dx.doi.org/10.1021/bi060837s; PMID: 16893191
  • Amijee H, Bate C, Williams A, Virdee J, Jeggo R, Spanswick D, Scopes DI, Treherne JM, Mazzitelli S, Chawner R, et al. The N-methylated peptide SEN304 powerfully inhibits Aβ(1-42) toxicity by perturbing oligomer formation. Biochemistry 2012; 51:8338 - 52; http://dx.doi.org/10.1021/bi300415v; PMID: 23025847
  • Matharu B, El-Agnaf O, Razvi A, Austen BM. Development of retro-inverso peptides as anti-aggregation drugs for β-amyloid in Alzheimer’s disease. Peptides 2010; 31:1866 - 72; http://dx.doi.org/10.1016/j.peptides.2010.06.033; PMID: 20633587
  • Parthsarathy V, McClean PL, Hölscher C, Taylor M, Tinker C, Jones G, Kolosov O, Salvati E, Gregori M, Masserini M, et al. A novel retro-inverso peptide inhibitor reduces amyloid deposition, oxidation and inflammation and stimulates neurogenesis in the APPswe/PS1ΔE9 mouse model of Alzheimer’s disease. PLoS One 2013; 8:e54769; http://dx.doi.org/10.1371/journal.pone.0054769; PMID: 23382963
  • Frydman-Marom A, Rechter M, Shefler I, Bram Y, Shalev DE, Gazit E. Cognitive-performance recovery of Alzheimer’s disease model mice by modulation of early soluble amyloidal assemblies. Angew Chem Int Ed Engl 2009; 48:1981 - 6; http://dx.doi.org/10.1002/anie.200802123; PMID: 19035593
  • Holmes C, Boche D, Wilkinson D, Yadegarfar G, Hopkins V, Bayer A, Jones RW, Bullock R, Love S, Neal JW, et al. Long-term effects of Abeta42 immunisation in Alzheimer’s disease: follow-up of a randomised, placebo-controlled phase I trial. Lancet 2008; 372:216 - 23; http://dx.doi.org/10.1016/S0140-6736(08)61075-2; PMID: 18640458
  • Sperling RA, Aisen PS, Beckett LA, Bennett DA, Craft S, Fagan AM, Iwatsubo T, Jack CR Jr., Kaye J, Montine TJ, et al. Toward defining the preclinical stages of Alzheimer’s disease: recommendations from the National Institute on Aging-Alzheimer’s Association workgroups on diagnostic guidelines for Alzheimer’s disease. Alzheimers Dement 2011; 7:280 - 92; http://dx.doi.org/10.1016/j.jalz.2011.03.003; PMID: 21514248
  • Crescenzi O, Tomaselli S, Guerrini R, Salvadori S, D’Ursi AM, Temussi PA, Picone D. Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain. Eur J Biochem 2002; 269:5642 - 8; http://dx.doi.org/10.1046/j.1432-1033.2002.03271.x; PMID: 12423364

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