Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation

Abedini, 2007, A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor, J. Am. Chem. Soc., 129, 11300, 10.1021/ja072157y

Acx, 2014, Signature amyloid β profiles are produced by different γ-secretase complexes, J. Biol. Chem., 289, 4346, 10.1074/jbc.M113.530907

Ahmed, 2010, Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils, Nat. Struct. Mol. Biol., 17, 561, 10.1038/nsmb.1799

Arosio, 2014, Chemical kinetics for drug discovery to combat protein aggregation diseases, Trends Pharmacol. Sci., 35, 127, 10.1016/j.tips.2013.12.005

Azzarito, 2013, Inhibition of α-helix-mediated protein-protein interactions using designed molecules, Nat. Chem., 5, 161, 10.1038/nchem.1568

Bhardwaj, 2016, Accurate de novo design of hyperstable constrained peptides, Nature, 538, 329, 10.1038/nature19791

Bieschke, 2012, Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils, Nat. Chem. Biol., 8, 93, 10.1038/nchembio.719

Caputo, 1989, The amyloid proteins of Alzheimer’s disease as potential targets for drug therapy, Neurobiol. Aging, 10, 451, 10.1016/0197-4580(89)90096-1

Cheng, 2012, Amyloid β-sheet mimics that antagonize protein aggregation and reduce amyloid toxicity, Nat. Chem., 4, 927, 10.1038/nchem.1433

Cheng, 2013, The supramolecular chemistry of β-sheets, J. Am. Chem. Soc., 135, 5477, 10.1021/ja3088407

Chiti, 2006, Protein misfolding, functional amyloid, and human disease, Annu. Rev. Biochem., 75, 333, 10.1146/annurev.biochem.75.101304.123901

Colletier, 2011, Molecular basis for amyloid-β polymorphism, Proc. Natl. Acad. Sci. U S A, 108, 16938, 10.1073/pnas.1112600108

Dobson, 2017, The amyloid phenomenon and its links with human disease, Cold Spring Harb. Perspect. Biol., 9, a023648, 10.1101/cshperspect.a023648

Ehrnhoefer, 2008, EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers, Nat. Struct. Mol. Biol., 15, 558, 10.1038/nsmb.1437

Eisenberg, 2012, The amyloid state of proteins in human diseases, Cell, 148, 1188, 10.1016/j.cell.2012.02.022

Fawzi, 2011, Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR, Nature, 480, 268, 10.1038/nature10577

Fitzpatrick, 2017, Cryo-EM structures of tau filaments from Alzheimer’s disease, Nature, 547, 185, 10.1038/nature23002

Gremer, 2017, Fibril structure of amyloid-β1–42 by cryo-electron microscopy, Science, 358, 116, 10.1126/science.aao2825

Haass, 2007, Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid β-peptide, Nat. Rev. Mol. Cell Biol., 8, 101, 10.1038/nrm2101

Hamley, 2012, The amyloid β peptide: a chemist’s perspective role in Alzheimer’s and fibrillization, Chem. Rev., 112, 5147, 10.1021/cr3000994

Han, 2018, Toward a rational design to regulate β-amyloid fibrillation for alzheimer’s disease treatment, ACS Chem. Neurosci., 9, 198, 10.1021/acschemneuro.7b00477

Härd, 2012, Inhibition of amyloid formation, J. Mol. Biol., 421, 441, 10.1016/j.jmb.2011.12.062

Huang, 2016, The coming of age of de novo protein design, Nature, 537, 320, 10.1038/nature19946

Huang, 2014, Maintenance of amyloid β peptide homeostasis by artificial chaperones based on mixed-shell polymeric micelles, Angew. Chem. Int. Ed. Engl., 53, 8985, 10.1002/anie.201400735

Jan, 2008, The ratio of monomeric to aggregated forms of Aβ40 and Aβ42 is an important determinant of amyloid-β aggregation, fibrillogenesis, and toxicity, J. Biol. Chem., 283, 28176, 10.1074/jbc.m803159200

Jiang, 2013, Structure-based discovery of fiber-binding compounds that reduce the cytotoxicity of amyloid β, Elife, 2, e00857, 10.7554/eLife.00857

Johnson, 2013, α-Helix mimicry with α/β-peptides, Methods Enzymol., 523, 407, 10.1016/B978-0-12-394292-0.00019-9

Kaspar, 2013, Future directions for peptide therapeutics development, Drug Discov. Today, 18, 807, 10.1016/j.drudis.2013.05.011

Knowles, 2009, An analytical solution to the kinetics of breakable filament assembly, Science, 326, 1533, 10.1126/science.1178250

Koo, 1999, Amyloid diseases: abnormal protein aggregation in neurodegeneration, Proc. Natl. Acad. Sci. U S A, 96, 9989, 10.1073/pnas.96.18.9989

Kreutzer, 2017, Stabilization, assembly, and toxicity of trimers derived from Aβ, J. Am. Chem. Soc., 139, 966, 10.1021/jacs.6b11748

Kummer, 2014, Truncated and modified amyloid-β species, Alzheimers. Res. Ther., 6, 28, 10.1186/alzrt258

Kuperstein, 2010, Neurotoxicity of Alzheimer’s disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio, EMBO J., 29, 3408, 10.1038/emboj.2010.211

Ladiwala, 2012, Rational design of potent domain antibody inhibitors of amyloid fibril assembly, Proc. Natl. Acad. Sci. U S A, 109, 19965, 10.1073/pnas.1208797109

Lawrence, 1993, Shape complementarity at protein/protein interfaces, J. Mol. Biol., 234, 946, 10.1006/jmbi.1993.1648

Leaver-Fay, 2011, ROSETTA3: an object-oriented software suite for the simulation and design of macromolecules, Meth. Enzymol., 487, 545, 10.1016/B978-0-12-381270-4.00019-6

Lee, 2014, Supramolecular inhibition of amyloid fibrillation by cucurbituril, Angew. Chem. Int. Ed. Engl., 53, 7461, 10.1002/anie.201402496

Lee, 1991, A68: a major subunit of paired helical filaments and derivatized forms of normal tau, Science, 251, 675, 10.1126/science.1899488

Lewczuk, 2004, Neurochemical diagnosis of Alzheimer’s dementia by CSF Aβ42, Aβ42/Aβ40 ratio and total tau, Neurobiol. Aging, 25, 273, 10.1016/S0197-4580(03)00086-1

Li, 2018, Differentialmodulation of the aggregation of n-terminal truncated aβ via cucurbiturils, Chem. Eur. J., 24, 13647, 10.1002/chem.201802655

Liu, 2012, Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates, Proc. Natl. Acad. Sci. U S A, 109, 20913, 10.1073/pnas.1218792109

Lu, 2013, Molecular structure of β-amyloid fibrils in Alzheimer’s disease brain tissue, Cell, 154, 1257, 10.1016/j.cell.2013.08.035

Meisl, 2014, Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides, Proc. Natl. Acad. Sci. U S A, 111, 9384, 10.1073/pnas.1401564111

Mowery, 2009, Structure-activity relationships among random nylon-3 copolymers that mimic antibacterial host-defense peptides, J. Am. Chem. Soc., 131, 9735, 10.1021/ja901613g

Murray, 2017, Structure of FUS protein fibrils and its relevance to self-assembly and phase separation of low-complexity domains, Cell, 171, 615.e16, 10.1016/j.cell.2017.08.048

Necula, 2007, Small molecule inhibitors of aggregation indicate that amyloid β oligomerization and fibrillization pathways are independent and distinct, J. Biol. Chem., 282, 10311, 10.1074/jbc.m608207200

Palhano, 2013, Toward the molecular mechanism(s) by which EGCG treatment remodels mature amyloid fibrils, J. Am. Chem. Soc., 135, 7503, 10.1021/ja3115696

Paravastu, 2008, Molecular structural basis for polymorphism in Alzheimer’s β-amyloid fibrils, Proc. Natl. Acad. Sci. U S A, 105, 18349, 10.1073/pnas.0806270105

Riek, 2016, The activities of amyloids from a structural perspective, Nature, 539, 227, 10.1038/nature20416

Salveson, 2016, X-ray crystallographic structure of oligomers formed by a toxic β-hairpin derived from α-synuclein: trimers and higher-order oligomers, J. Am. Chem. Soc., 138, 4458, 10.1021/jacs.5b13261

Sánchez, 2011, Aβ40 and Aβ42 amyloid fibrils exhibit distinct molecular recycling properties, J. Am. Chem. Soc., 133, 6505, 10.1021/ja1117123

Sawaya, 2007, Atomic structures of amyloid cross-β spines reveal varied steric zippers, Nature, 447, 453, 10.1038/nature05695

Seidler, 2018, Structure-based inhibitors of tau aggregation, Nat. Chem., 10, 170, 10.1038/nchem.2889

Sevigny, 2016, The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease, Nature, 537, 50, 10.1038/nature19323

Sievers, 2011, Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation, Nature, 475, 96, 10.1038/nature10154

Spillantini, 1997, α-synuclein in lewy bodies, Nature, 388, 839, 10.1038/42166

Szaruga, 2017, Alzheimer’s-causing mutations shift Aβ length by destabilizing γ-secretase-Aβn interactions, Cell, 170, 443.e14, 10.1016/j.cell.2017.07.004

Tuttle, 2006, Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein, Nat. Struct. Mol. Biol., 23, 409, 10.1038/nsmb.3194

Xue, 2008, Systematic analysis of nucleation-dependent polymerization reveals new insights into the mechanism of amyloid self-assembly, Proc. Natl. Acad. Sci. U S A, 105, 8926, 10.1073/pnas.0711664105

Zheng, 2013, A hydrophobic surface is essential to inhibit the aggregation of a tau-protein-derived hexapeptide, J. Am. Chem. Soc., 135, 6846, 10.1021/ja310817d

Zheng, 2011, Macrocyclic β-sheet peptides that inhibit the aggregation of a tau-protein-derived hexapeptide, J. Am. Chem. Soc., 133, 3144, 10.1021/ja110545h